Publications

Theses

Undergraduate Honors Thesis, Carleton College, 1963, “Sulfato and Oxalatochromium (III) Complexes”

Ph.D. Thesis, Harvard University, 1969, “Proton Magnetic Resonance Studies of the Structure and Binding Sites of Staphylococcal Nuclease”

Book Review

J. L. Markley, “Enzyme Nomenclature 1984,” J. Amer. Chem. Soc. 109, 7589 (1987).

Edited Volumes

J. L. Markley, C. A. Royer, and D. Northrop, Eds., HighPressure Effects in Molecular Biophysics and Enzymology, Oxford University Press, New York, 1996.

J. L. Markley and S. J. Opella, Eds., Biological NMR Spectroscopy, Oxford University Press, New York, 1996.

Research Articles and Reviews

1. J. L. Markley, D. H. Meadows, and O. Jardetzky, “Nuclear Magnetic Resonance Studies of HelixCoil Transitions in Polyamino Acids,” J. Mol. Biol. 27, 2540 (1967).

2. D. H. Meadows, J. L. Markley, J. S. Cohen, and O. Jardetzky, “Nuclear Magnetic Resonance Studies of the Structure and Binding Sites of Enzymes, I. Histidine Residues,” Proc. Natl. Acad. Sci. USA 58, 13071313 (1967).

3. J. L. Markley, I. Putter, and O. Jardetzky, “HighResolution Nuclear Magnetic Resonance Spectra of Selectively Deuterated Staphylococcal Nuclease,” Science 161, 12491251 (1968).

4. J. L. Markley, I. Putter, and O. Jardetzky, “Application of Nuclear Magnetic Resonance in Biochemistry: An Analysis of the Aromatic Region of the Proton Magnetic Resonance Spectrum of Staphylococcal Nuclease,” Fresenius' Zh. Anal. Chem. 243, 367374 (1968).

5. J. L. Markley, T. C. Hollocher, A. S. Brill, and O. Jardetzky, “Magnetic Susceptibility and Magnetic Resonance,” Phys. Tech. Biol. Res. 2B, 117223 (1969).

6. I. Putter, A. Barreto, J. L. Markley, and O. Jardetzky, “Nuclear Magnetic Resonance Studies of the Structure and Binding Sites of Enzymes, X. Preparation of Selectively Deuterated Analogs of Staphylococcal Nuclease,” Proc. Natl. Acad. Sci. USA 64, 13961403 (1969).

7. I. Putter, J. L. Markley, and O. Jardetzky, “Nuclear Magnetic Resonance Studies of the Structure and Binding Sites of Enzymes, XI. Characterization of Selectively Deuterated Analogs of Staphylococcal Nuclease,” Proc. Natl. Acad. Sci. USA 65, 395401 (1970).

8. J. L. Markley, M. N. Williams, and O. Jardetzky, “Nuclear Magnetic Resonance Studies of the Structure and Binding Sites of Enzymes, XII. A Conformational Equilibrium in Staphylococcal Nuclease Involving a Histidine Residue,” Proc. Natl. Acad. Sci.USA 65, 645651 (1970).

9. O. Jardetzky and J. L. Markley, “Nuclear Magnetic Resonance Studies on Selectively Deuterated Staphylococcal Nuclease,” Farmaco, Ed. Sci. 25, 894897 (1970).

10. J. L. Markley and O. Jardetzky, “Nuclear Magnetic Resonance Studies of the Structure and Binding Sites of Enzymes, XIV. Inhibitor Binding to Staphylococcal Nuclease,” J. Mol. Biol. 50, 223233 (1970).

11. J. L. Markley, W. J. Horsely, and M. P. Klein, “SpinLattice Relaxation Measurements in Slowly Relaxing Complex Spectra,” J. Chem. Phys. 55, 36043605 (1971).

12. O. Jardetzky, J. Thielmann, Y. Arata, J. L. Markley, and M. N. Williams, “Tentative Sequential Model for the Unfolding and Refolding of Staphylococcal Nuclease at High pH,” Cold Spring Harbor Symp. Quant. Biol. 36, 257261 (1972).

13. J. L. Markley, “HighResolution Proton Magnetic Resonance Spectroscopy of Selectively Deuterated Enzymes,” Methods Enzymol. 26, 605627 (1972).

14. J. L. Markley, “Nuclear Magnetic Resonance Studies of Trypsin Inhibitors. Histidines of Virgin and Modified Soybean Trypsin Inhibitors (Kunitz),” Biochemistry 12, 22452250 (1973).

15. J. L. Markley, “HighResolution Proton Magnetic Resonance Studies of Two Trypsin Inhibitors: Soybean Trypsin Inhibitor (Kunitz) and Ovomucoid (Hen Egg White),” Ann. N.Y. Acad. Sci.USA 222, 347373 (1973).

16. J. L. Markley and S.M. Cheung, “Differential Exchange of the C2Hydrogens of Histidine Side Chains in Native Proteins: Proposed General Technique for the Assignment of Histidine NMR Peaks in Proteins,” In Proc. Int. Conf. On Stable Isotopes in Chem., Biol., and Med., Argonne, IL, May 1973, U.S. Atomic Energy Commission CONF 730525, 103118 (1973).

17. J. L. Markley, “Observation of Histidine Residues in Proteins by Means of Nuclear Magnetic Resonance Spectroscopy,” Accts. Chem. Res. 8, 7080 (1975).

18. J. L. Markley, W.R. Finkenstadt, H. Dugas, P. Leduc, and D.R. Drapeau, “Proton Magnetic Resonance Titration Curves of the Three Histidine Residues of Staphylococcal Protease,” Biochemistry 14, 9981005 (1975).

19. J. L. Markley and I. Kato, “Assignment of the Histidine Proton Magnetic Resonance Peaks of Soybean Trypsin Inhibitor (Kunitz) by a Differential Deuterium Exchange Technique,” Biochemistry 14, 32343237 (1975).

20. J. L. Markley, “Correlation Proton Magnetic Resonance Studies at 250 MHz of Bovine Pancreatic Ribonuclease. I. Reinvestigation of Histidine Peak Assignments,” Biochemistry 14, 35463554 (1975).

21. J. L. Markley, “Correlation Proton Magnetic Resonance Studies at 250 MHz of Bovine Pancreatic Ribonuclease. II. pH and InhibitorInduced Conformational Transitions Affecting Histidine48 and One Tyrosine Residue of Ribonuclease A,” Biochemistry 14, 35543561 (1975).

22. J. L. Markley and W. R. Finkenstadt, “Correlation Proton Magnetic Resonance Studies at 250 MHz of Bovine Pancreatic Ribonuclease. III. Mutual Electrostatic Interaction Between Histidine Residues 12 and 119,” Biochemistry 14, 35623566 (1975).

23. J. L. Markley, E. L. Ulrich, S. P. Berg, and D. W. Krogmann, “Nuclear Magnetic Resonance Studies of the Copper Binding Sites of Blue Copper Proteins: Oxidized, Reduced, and Apoplastocyanin,” Biochemistry 14, 44284433 (1975).

24. J. L. Markley and M. P. Porubcan, “The Chargerelay System of Serine Proteinases: Proton Magnetic Resonance Titration Studies of the Four Histidines of Porcine Trypsin,” J. Mol. Biol. 102, 487509 (1976).

25. J. L. Markley, E. L. Ulrich, and D. W. Krogmann, “Spinach Plastocyanin: Comparison of Reduced and Oxidized Forms by Natural Abundance Carbon13 Nuclear Magnetic Resonance Spectroscopy,” Biochem. Biophys. Res. Commun. 78, 106114 (1977).

26. J. L. Markley and I. B. Ibañez, “Zymogen Activation in Serine Proteinases. Proton Magnetic Resonance pH Titration Studies of the Two Histidines of Bovine Chymotrypsinogen A and Chymotrypsin Aα,” Biochemistry 17, 46274640 (1978).

27. M. A. Porubcan, D. E. Neves, S. K. Rausch, and J. L. Markley, “Active Site in Zymogens, Proton Magnetic Resonance pH Titration Curves of Histidine57 in Porcine and Bovine Trypsinogens and in their Complexes with Bovine Pancreatic Trypsin Inhibitors (Kunitz),” Biochemistry 17, 46404647 (1978).

28. J. L. Markley, “Hydrogen Bonds in Serine Proteinases and their Complexes with Protein Proteinase Inhibitors. Proton Nuclear Magnetic Resonance Studies,” Biochemistry 17, 46484656 (1978).

29. E. L. Ulrich and J. L. Markley, “Blue Copper Proteins: Nuclear Magnetic Resonance Investigations,” Coord. Chem. Rev. 27, 109140 (1978).

30. J. L. Markley, “Catalytic Groups of Serine Proteinases. NMR Investigations,” In Magnetic Resonance Studies in Biology, (R.G. Shulman, Ed.) Academic Press, New York, pp. 397461 (1979).

31. M. A. Porubcan, W. M. Westler, I. B. Ibañez, and J. L. Markley, “(Diisopropylphosphoryl)serine Proteinases. Proton and Phosphorus31 Nuclear Magnetic ResonancepH Titration Studies,” Biochemistry 18, 41084116 (1979).

32. M. W. Baillargeon, M. Laskowski, Jr., D. E. Neves, M. A. Porubcan, R. E. Santini, and J. L. Markley, “Soybean Trypsin Inhibitor (Kunitz) and its Complex with Trypsin. Carbon13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine,” Biochemistry 19, 57035710 (1980).

33. J. L. Markley, D. E. Neves, W. M. Westler, I. B. Ibañez, M. A. Porubcan, and M. W. Baillargeon, “Nuclear Magnetic Resonance Studies of Serine Proteinases,” Dev. Biochem. 10, 3161 (1980).

34. D. C. McCain and J. L. Markley, “Phosphorus31 SpinLattice Relaxation in Aqueous Orthophosphate Solutions,” J. Am. Chem. Soc. 102, 55595565 (1980).

35. T.M. Chan, E. L. Ulrich, and J. L. Markley, “Two IronTwo Sulfur Ferredoxin From Spinach and Cyanobacteria. NMR Studies of Their Structures and Redox Sites,” In Photosynthesis II. Electron Transport and Photophosphorylation, (G. Akoyunoglou, Ed.) Balaban Int. Science Services, Philadelphia, pp. 697704 (1981).

36. E. L. Ulrich, D. W. Krogmann, and J. L. Markley, “Cytochrome c533: Heme Environment and Unpaired Electron Distribution as Determined by1H NMR Spectroscopy at 360 MHz,” In Photosynthesis II. Electron Transport and Photophosphorylation, (G. Akoyunoglou, Ed.) Balaban Int. Science Services, Philadelphia, pp. 583590 (1981).

37. M. A. E. Sallam, R. L. Whistler, and J. L. Markley, “6Chloro3ßDErythrofuranosyl1Phenyl and 1pTolylPyrazolo[3,4b]Quinoxaline,” Carbohydr. Res. 87, 8797 (1980).

38. M. A. E. Sallam, E. I. A. Hegazy, R. L. Whistler, and J. L. Markley, “Studies on 3,6AnhydroOsazones of Hexoses: Characterization and Anomeric Configuration,” Carbohydr. Res. 83, C1C4 (1980).

39. J. L. Markley, F. Travers, and C. Balny, “Lack of Evidence for a Tetrahedral Intermediate in the Hydrolysis of Nitroanilide Substrates by Serine Proteinases,” Eur. J. Biochem. 120, 477485 (1981).

40. D. C. McCain, R. Virudachalam, J. L. Markley, S. S. AbdelMeguid, and M. G. Rossmann, “Carbon13 NMR Study of Southern Bean Mosaic Virus,” Virology 117, 501503 (1982).

41. W. M. Westler, J. L. Markley, and W. W. Bachovchin, “Proton NMR Spectroscopy of the Active Site Histidine of αLytic Proteinase. Effects of Adjacent 13C and 15N Labels,” FEBS Lett. 138, 233235 (1982).

42. E. L. Ulrich, D. W. Krogmann, and J. L. Markley, “Structure and Heme Environment of Ferrocytochrome c553 from 1H NMR Studies,” J. Biol. Chem. 257, 93569364 (1982).

43. T. Ogino, C. Garner, J. L. Markley, and K. M. Herrmann, “Biosynthesis of Aromatic Compounds: 13C NMR Spectroscopy of Whole Escherichia coli Cells,” Proc. Natl. Acad. Sci. USA 79, 58285832 (1982).

44. T.M. Chan and J. L. Markley, “Heteronuclear (1H, 13C) TwoDimensional Chemical Shift Correlation NMR Spectroscopy of a Protein. Ferredoxin from Anabaena variabilis,” J. Am. Chem. Soc. 104, 40104011 (1982).

45. T.M. Chan, W. M. Westler, R. E. Santini, and J. L. Markley, “Carbon13 NMR Subspectra of a Protein Based on the Number of Attached Protons. Ferredoxin from Anabaena variabilis,” J. Am. Chem. Soc. 104, 40084010 (1982).

46. T. Ogino, D. H. Croll I. Kato, and J. L. Markley, “Properties of Conserved Amino Acid Residues in Tandem Homologous Protein Domains. Hydrogen1 Nuclear Magnetic Resonance Studies of the Histidines of Chicken Ovomucoid,” Biochemistry 21, 34523460 (1982).

47. M. Bárány, D. D. Doyle, G. Graff, W. M. Westler, and J. L. Markley, “Changes in the Natural Abundance 13C NMR Spectra of Intact Frog Muscle upon Storage and Caffeine Contracture,” J. Biol. Chem. 257, 27412743 (1982).

48. D. C. McCain, R. Virudachalam, R. E. Santini, S. S. AbdelMeguid, and J. L. Markley, “Phosphorus31 Nuclear Magnetic Resonance Study of Internal Motion in the RNA of Southern Bean Mosaic Virus,” Biochemistry 21, 53905397 (1982).

49. J. A. Blaszak, E. L. Ulrich, J. L. Markley, and D. R. McMillin, “HighResolution Proton Nuclear Magnetic Resonance Studies of the Nickel(II) Derivative of Azurin,” Biochemistry 24, 62536258 (1982).

50. M. A. E. Sallam, E. I. A. Hegazy, R. L. Whistler, J. L. Markley, and D. H. Croll, “Studies on 3Epimeric L2Hexulose Phenylosazones. Structure and Anomeric Configuration of the 3,6AnhydroOsazone Derivatives Obtained from Lxylo and Llyxo2Hexulose Phenylosazone,” Carbohydr. Res. 102, 197206 (1982).

51. E. L. Ulrich, W. M. Westler, and J. L. Markley, “Reassignments in the 1H NMR Spectrum of Flavin Adenine Dinucleotide by TwoDimensional Homonuclear Chemical Shift Correlation,” Tet. Lett. 24, 473476 (1983).

52. T.M. Chan and J. L. Markley, “Nuclear Magnetic Resonance Studies of TwoIronTwoSulfur Ferredoxins. 1. Properties of the Histidine Residues,” Biochemistry 22, 59825987 (1983).

53. T.M. Chan, M. A. Hermodson, E. L. Ulrich, and J. L. Markley, “Nuclear Magnetic Resonance Studies of TwoIronTwoSulfur Ferredoxins. 2. Determination of the Sequence of Anabaena variabilis Ferredoxin II, Assignment of Aromatic Resonances in Proton Spectra, and Effects of Chemical Modifications,” Biochemistry 22, 59885995 (1983).

54. T.M. Chan and J. L. Markley, “Nuclear Magnetic Resonance Studies of TwoIronTwo Sulfur Ferredoxins. 3. Heteronuclear (13C, 1H) TwoDimensional NMR Spectra, 13C Peak Assignments, and 13C Relaxation Measurements,” Biochemistry 22, 59966002 (1983).

55. T.M. Chan, E. L. Ulrich, and J. L. Markley, “Nuclear Magnetic Resonance Studies of TwoIronTwoSulfur Ferredoxins. 4. Interactions with Redox Partners,” Biochemistry 22, 60026007 (1983).

56. T.M. Chan and J. L. Markley, “Nuclear Magnetic Resonance Studies of TwoIronTwoSulfur Ferredoxins. 5. HyperfineShifted Peaks in Hydrogen1 and Carbon13 Spectra,” Biochemistry 22, 60086010 (1983).

57. M. Bárány, D. D. Doyle, G. Graff, W. M. Westler, and J. L. Markley, “Natural Abundance 13C NMR Spectra of Human Muscle, Normal and Diseased,” J. Mag. Reson. Med. 1, 3043 (1984).

58. R. Virudachalam, K. Sitaraman, K. L. Heuss, J. L. Markley, and P. Argos, “Evidence for pHInduced Release of RNA from Belladonna Mottle Virus and the Stabilizing Effect of Polyamines and Cations,” Virology 130, 351359 (1983).

59. R. Virudachalam, K. Sitaraman, K. L. Heuss, P. Argos, and J. L. Markley, “Carbon13 and Proton Nuclear Magnetic Resonance Spectroscopy of Plant Viruses: Evidence for ProteinNucleic Acid Interactions in Belladonna Mottle Virus and Detection of Polyamines in Turnip Yellow Mosaic Virus,” Virology 130, 360371 (1983).

60. C. L. Kojiro and J. L. Markley, “Connectivity of Proton and Carbon Spectra of the Blue Copper Protein, Plastocyanin, Established by TwoDimensional Nuclear Magnetic Resonance,” FEBS Lett. 162, 5256 (1983).

61. J. L. Markley, W. M. Westler, T.M. Chan, C. L. Kojiro, and E. L. Ulrich, “Two Dimensional NMR Approaches to the Study of Protein Structure and Function,” Federation Proc. 43, 26482656 (1984).

62. E. L. Ulrich, E.M. M. John, G. R. Gough, M. J. Brunden, P. T. Gilham, W. M. Westler, and J. L. Markley, “Imino Proton Assignments in the Proton Nuclear Magnetic Resonance Spectrum of the λ Phage OR3 Deoxyribonucleic Acid Fragment,” Biochemistry 22, 43624365 (1983).

63. J. L. Markley and E. L. Ulrich, “Detailed Analysis of Protein Structure and Function by NMR Spectroscopy: Survey of Resonance Assignments,” Ann. Rev. Biophys. Bioeng. 13, 493521 (1984).

64. G. I. Rhyu, W. J. Ray, Jr., and J. L. Markley, “EnzymeBound Intermediates in the Conversion of Glucose 1Phosphate to Glucose 6Phosphate by Phosphoglucomutase. Phosphorus NMR Studies,” Biochemistry 23, 252260 (1984).

65. D. C. McCain, T. C. Selig, Govindjee, and J. L. Markley, “Some Plant Leaves Have OrientationDependent EPR and NMR Spectra,” Proc. Nat. Acad. Sci. USA 81, 748752 (1984).

66. C. Arús, M. Bárány, W. M. Westler, and J. L. Markley, “Proton Nuclear Magnetic Resonance of Human Muscle Extracts,” Clinical Physiol. Biochem. 2, 4955 (1984).

67. C. Arús, M. Bárány, W. M. Westler, and J. L. Markley, “1H NMR of Intact Muscle at 11 T,” FEBS Lett. 165, 231237 (1984).

68. W. M. Westler, G. OrtizPolo, and J. L. Markley, “TwoDimensional 1H13C ChemicalShift Correlated Spectroscopy of a Protein at Natural Abundance,” J. Magn. Reson. 58, 354357 (1984).

69. C. Arús, M. Bárány, W. M. Westler, and J. L. Markley, “1H NMR of Intact Tissues at 11.1 T,” J. Magn. Reson. 57, 519525 (1984).

70. X. Wu, W. M. Westler, and J. L. Markley, “The Assignment of Imidazolium N1H Peaks in the 1H NMR Spectrum of a Protein by One and TwoDimensional NOE Experiments,” J. Magn. Reson. 59, 524529 (1984).

71. R. Virudachalam, M. Harrington, J. E. Johnson, and J. L. Markley, “1H, 13C, and 31P Nuclear Magnetic Resonance Studies of Cowpea Mosaic Virus: Detection and Exchange of Polyamines and Dynamics of the RNA,” Virology 141, 4350 (1985).

72. G. I. Rhyu, W. J. Ray, Jr., and J. L. Markley, “Multinuclear Magnetic Resonance Studies of Metal Ion Binding Sites of Phosphoglucomutase,” Biochemistry 24, 2536 2541 (1985).

73. R. Virudachalam, P. S. Low, P. Argos, and J. L. Markley, “Turnip Yellow Mosaic Virus and its Empty Capsid have Thermal Stabilities with Opposite pH Dependence: Studies by Differential Scanning Calorimetry and 31P Nuclear Magnetic Resonance Spectroscopy,” Virology 146, 213220 (1985).

74. E. L. Ulrich, M. E. Girvin, W. A. Cramer, and J. L. Markley, “Location and Mobility of Ubiquinones of Different Chain Lengths in Artificial Membrane Vesicles,” Biochemistry 24, 25012508 (1985).

75. G. I. Rhyu, W. J. Ray, and J. L. Markley, “ActiveSite Serine Phosphate and Histidine Residues of Phosphoglucomutase: pH Titration Studies Monitored by 1H and 31P NMR Spectroscopy,” Biochemistry 24, 47464753 (1985).

76. D. C. McCain and J. L. Markley, “Water Permeability of Chloroplast Envelope Membranes: In Vivo Measurement by SaturationTransfer NMR,” FEBS Lett. 183, 353 358 (1985).

77. D. H. Live, C. L. Kojiro, D. Cowburn, and J. L. Markley, “Identification of Proton NMR Signals from the Metal Ligands in CadmiumSubstituted Plastocyanin via Two Dimensional MultipleQuantum Detection in the Absence of Explicitly Resolved 1H113Cd Coupling,” J. Am. Chem. Soc. 107, 30433045 (1985).

78. R. Virudachalam and J. L. Markley, “Nuclear Magnetic Resonance Studies of Spherical Plant Viruses,” Biophys. J. 49, 3335 (1986).

79. D. C. McCain and J. L. Markley, “A Theory and a Model for Interpreting the Proton Nuclear Magnetic Resonance Spectra of Water in Plant Leaves,” Biophys. J. 48, 687694 (1985).

80. R. Virudachalam, M. Harrington, and J. L. Markley, “Thermal Stability of Cowpea Mosaic Virus Components: Differential Scanning Calorimetry Studies,” Virology 146, 138140 (1985).

81. J. L. Markley, D. H. Croll, R. Krishnamoorthi, G. OrtizPolo, W. M. Westler, W. C. Bogard, Jr., and M. Laskowski, Jr., “One and TwoDimensional NMR Spectral Analysis of the Consequences of Single Amino Acid Replacements in Proteins,” J. Cellular Biochem. 30, 291309 (1986).

82. R. Krishnamoorthi, J. L. Markley, M. A. Cusanovich, and C. T. Przysiecki, “Hydrogen1 Nuclear Magnetic Resonance Investigation of Clostridium pasteurianum Rubredoxin: Previously Unobserved Signals,” Biochemistry 25, 5054 (1986).

83. R. Krishnamoorthi, J. L. Markley, M. A. Cusanovich, C. T. Przysiecki, and T. E. Meyer, “Hydrogen1 Nuclear Magnetic Resonance Investigation of HighPotential IronSulfur Proteins from Ectothiorhodospira halophila and Ectothiorhodospira vacuolata: A Comparative Study of HyperfineShifted Resonances,” Biochemistry 25, 6067 (1986).

84. J. L. Markley, “One and Twodimensional NMR Spectroscopic Investigations of the Consequences of Amino Acid Replacements in Proteins,” In Protein Engineering (Dale L. Oxender, Ed.) New York: Alan R. Liss, pp. 1533 (1987).

85. J. L. Markley, T.M. Chan, R. Krishnamoorthi, and E. L. Ulrich, “Nuclear Magnetic Resonance Studies of StructureFunction Relationships in IronSulfur Proteins,” In Frontiers of IronSulfur Protein Research, (H. Matsubara et al. Eds.), Japan Sci. Soc. Press, Tokyo/SpringerVerlag, Berlin, pp. 167181 (1986).

86. G. OrtizPolo, R. Krishnamoorthi, J. L. Markley, D. H. Live, D. G. Davis, and D. Cowburn, “NaturalAbundance 15N NMR Studies of Turkey Ovomucoid Third Domain. Assignment of Peptide 15N Resonances to the Residues at the Reactive Site Region via ProtonDetected Multiple Quantum Coherence,” J. Magn. Res. 68, 303310 (1986).

87. C. Arús, W. M. Westler, M. Bárány, and J. L. Markley, “Observation of the Terminal Methyl Group in Fatty Acids of the Linolenic Series by Means of a New 1H NMR Pulse Sequence Providing Spectral Editing and Solvent Suppression. Application to Excised Frog Muscle and Rat Brain,” Biochemistry 25, 33463351 (1986).

88. D. C. McCain and J. L. Markley, “Rotational Spectral Density Functions for Aqueous Sucrose: Experimental Determination Using 13C NMR,” J. Am. Chem. Soc. 108, 42594264 (1986).

89. D. C. McCain and J. L. Markley, “The Solution Conformation of Sucrose: Concentration and Temperature Dependence,” Carbohyd. Res. 152, 7380 (1986).

90. B. Tobias and J. L. Markley, “Carbon13 Relaxation of [113C]Acetylchymotrypsin Dissolved in a Cryosolvent at Subzero Temperatures,” J. Magn. Reson. 69, 381385 (1986).

91. D. C. McCain and J. L. Markley, “Internal Motions of the Three Hydroxymethyl Groups in Aqueous Sucrose,” J. Magn. Reson. 73, 244251 (1987).

92. Zs. Zolnai, S. Macura, and J. L. Markley, “An Efficient Method for Eliminating Noise in TwoDimensional Nuclear Magnetic Resonance Spectra,” Computer Enhanced Spectroscopy 3, 141145 (1986).

93. B. J. Stockman and J. L. Markley, “Flavodoxin from Anabaena 7120: Uniform N15 Enrichment and Nitrogen15, and Phosphorus31 NMR Investigations of the FMN Binding Site in the Reduced and Oxidized States,” In Flavins and Flavoproteins, (D.E. Edmondson and D.B. McCormick, Eds.) W. de Gruyter, Berlin, pp. 275278 (1987).

94. D. C. McCain, J. Croxdale, and J. L. Markley, “Water is Allocated Differently to Chloroplasts in Sun and Shade Leaves,” Plant Physiol. 86, 1618 (1988).

95. B. J. Stockman, W. M. Westler, E. S. Mooberry, and J. L. Markley, “Flavodoxin from Anabaena 7120: Uniform Nitrogen15 Enrichment and Hydrogen1, Nitrogen15, and Phosphorus31 NMR Investigations of the FMN Binding Site in the Reduced and Oxidized States,” Biochemistry 27, 136142 (1988).

96. A. T. Alexandrescu, D. A. Mills, E. L. Ulrich, M. Chinami, and J. L. Markley, “NMR Assignments of the Four Histidines of Staphylococcal Nuclease in Native and Denatured States,” Biochemistry 27, 21582165 (1988).

97. A. D. Robertson, W. M. Westler, and J. L. Markley, “TwoDimensional NMR Studies of Kazal Proteinase Inhibitors. 1. SequenceSpecific Assignments and Secondary Structure of Turkey Ovomucoid Third Domain,” Biochemistry 27, 25192529 (1988)

98. G. I. Rhyu and J. L. Markley, “TwoDimensional NMR Studies of Kazal Proteinase Inhibitors. 2. SequenceSpecific Assignments and Secondary Structure of Reactive Site Modified Turkey Ovomucoid Third Domain,” Biochemistry 27, 25292539 (1988).

99. D. C. McCain, E. L. Ulrich, and J. L. Markley, “NMR Relaxation Study of Flavin Mononucleotide Internal Motions in Staphylococcal Nuclease,” J. Magn. Reson. 80, 296305 (1988).

100. Zs. Zolnai, S. Macura, and J. L. Markley, “Compression of NMR Data. Application to TwoDimensional NMR Spectroscopy and Imaging,” J. Magn. Reson. 80, 6070 (1988).

101. D. C. McCain, J. Croxdale and J. L. Markley, “Thermal Damage to Chloroplast Envelope Membranes,” Plant Physiol. 90, 606609 (1989).

102. E. L. Ulrich, J. L. Markley, and Y. Kyogoku, “Creation of a Nuclear Magnetic Resonance Data Repository and Literature Database,” Prot. Seq. Data Anal. 2, 2337 (1989).

103. W. M. Westler, M. Kainosho, H. Nagao, N. Tomonaga, and J. L. Markley, “Two Dimensional NMR Strategies for CarbonCarbon Correlations and SequenceSpecific Assignments in Carbon13 Labeled Proteins,” J. Am. Chem. Soc. 110, 40934095 (1988).

104. B. J. Stockman, W. M. Westler, P. Darba, and J. L. Markley, “Detailed Analysis of Carbon13 NMR Spin Systems in a Uniformly Carbon13 Enriched Protein: Flavodoxin from Anabaena 7120,” J. Am. Chem. Soc. 110, 40954096 (1988).

105. B.H. Oh, W. M. Westler, P. Darba, and J. L. Markley, “Protein Carbon13 Spin Systems by a Single TwoDimensional Nuclear Magnetic Resonance Experiment,” Science 240, 908911 (1988).

106. W. M. Westler, B. J. Stockman, J. L. Markley, Y. Hosoya, Y. Miyake, and M. Kainosho, “Correlation of Carbon13 and Nitrogen15 Chemical Shifts in Uniformly Labeled Proteins by Heteronuclear TwoDimensional NMR Spectroscopy,” J. Am. Chem. Soc. 110, 62566258 (1988).

107. B. J. Stockman, M. D. Reily, W. M. Westler, E. L. Ulrich, and J. L. Markley, “Concerted TwoDimensional NMR Approaches to Hydrogen1, Carbon13, and Nitrogen15 Resonance Assignments in Proteins,” Biochemistry 28, 230236 (1989).

108. A. T. Alexandrescu, E. L. Ulrich, and J. L. Markley, “Hydrogen1 NMR Evidence for Three Interconverting Forms of Staphylococcal Nuclease: Effects of Mutations and Solution Conditions on their Distribution,” Biochemistry 28, 204211 (1989).

109. J. L. Markley, “TwoDimensional Nuclear Magnetic Resonance Spectroscopy of Proteins: an Overview,” Methods Enzymol. 176, 1264 (1989).

110. A. D. Robertson and J. L. Markley, “Methods of Proton Resonance Assignment for Proteins,” Biol. Magn. Reson. 9, 155176 (1990).

111. J. Fejzo, Zs. Zolnai, S. Macura, and J. L. Markley, “Analysis of Laboratory Frame and RotatingFrame CrossRelaxation Buildup Rates from Macromolecules,” J. Magn. Reson. 82, 518528 (1989).

112. Zs. Zolnai, S. Macura, and J. L. Markley, “Spline Method for Correcting Baseplane Distortions in TwoDimensional NMR Spectra,” J. Magn. Reson. 82, 496504 (1989).

113. C. B. Grissom and J. L. Markley, “Staphylococcal Nuclease ActiveSite Amino Acids: pH Dependence of Tyrosines and Arginines by 13C NMR and Correlation with Kinetic Studies,” Biochemistry 28, 21162124 (1989).

114. J. Alonso, C. Arús, W. M. Westler, and J. L. Markley, “TwoDimensional Correlated Spectroscopy (COSY) of Intact Frog Muscle: Spectral Pattern Characterization and Lactate Quantitation,” Magn. Reson. Med. 11, 316330 (1989).

115. B.H. Oh and J. L. Markley, “Complete Carbon13 Resonance Assignments of Tryptophan in LLysylLTryptophylLLysine by SingleBond and MultipleBond Correlated 1H13C TwoDimensional NMR,” Biopolymers 28, 18331837 (1989).

116. B.H. Oh, W. M. Westler, and J. L. Markley, “Carbon13 Spin System Directed Strategy for Assigning Cross Peaks in the COSY Fingerprint Region of a Protein,” J. Am. Chem. Soc. 111, 30833085 (1989).

117. D. C. McCain and J. L. Markley, “More Manganese Accumulates in Maple Sun Leaves than in Shade Leaves,” Plant Physiol. 90, 14171421 (1989).

118. E. S. Mooberry, B.H. Oh, and J. L. Markley, “Improvement of 13C15N ChemicalShift Correlation Spectroscopy by Implementing Time Proportional Phase Incrementation,” J. Magn. Reson. 85, 147149 (1989).

119. A. D. Robertson, G. I. Rhyu, W. M. Westler, and J. L. Markley, “Assignment of the 13CNMR Spectra of Virgin and ReactiveSite Modified Turkey Ovomucoid Third Domain,” Biopolymers 29, 461467 (1990).

120. B. J. Stockman and J. L. Markley, “StableIsotopeAssisted Protein NMR Spectroscopy in Solution,” In Advances in Biophysical Chemistry, Vol. 1 (Bush, C. A., Ed.), JAI Press Inc., Greenwich, Connecticut, pp. 146 (1990).

121. J. Wang, D. M. LeMaster, and J. L. Markley, “TwoDimensional 1H NMR Studies of Staphylococcal Nuclease: 1. Solution Structure of the (Nuclease H124L)Thymidine 3',5'BisphosphateCa2+ Ternary Complex,” Biochemistry 29, 88101 (1990).

122. J. Wang, A. P. Hinck, S. N. Loh, and J. L. Markley, “TwoDimensional 1H NMR Studies of Staphylococcal Nuclease: 2. SequenceSpecific Assignments of Carbon13 and Nitrogen15 Signals from the (Nuclease H124L)Thymidine 3',5'bisphosphateCa2+ Ternary Complex,” Biochemistry 29, 102113 (1990).

123. A. T. Alexandrescu, S. N. Loh, and J. L. Markley, “Chemical Exchange Spectroscopy Based on Carbon13. NMR Applications to Enzymology and Protein Folding,” J. Magn. Reson. 87, 523535 (1990).

124. S. E. Kornguth, M. E. Anderson, P. Turski, J. Sorenson, H. I. Robins, J. Cohen, A. Rappe, and J. L. Markley, “Glioblastoma Multiforme: MR Imaging at 1.5 and 9.4 T After Injection of PolylysineDTPAGd in Rats,” Am. J. Neuro. Radiol. 11, 313318 (1990).

125. M. H. Zehfus, M. D. Reily, E. L. Ulrich, W. M. Westler, and J. L. Markley, “1H, 13C, and 15N Resonance Assignments for a Ferrocytochrome c553 Heme by Multinuclear NMR Spectroscopy,” Arch. Biochem. Biophys. 276, 369373 (1990).

126. J. Fejzo, Zs. Zolnai, S. Macura, and J. L. Markley, “Quantitative Evaluation of TwoDimensional CrossRelaxation NMR Spectra of Proteins. Interproton Distances in Turkey Ovomucoid Third Domain,” J. Magn. Reson. 88, 93110 (1990).

127. J. L. Markley, B. R. Seavey, A. T. Alexandrescu, P. Darba, A. P. Hinck, S. N. Loh, C. W. McNemar, E. S. Mooberry, B.H. Oh, B. J. Stockman, J. Wang, W. M. Westler, M. H. Zehfus, and Zs. Zolnai, “Multinuclear Magnetic Resonance Spectroscopy of Proteins: Information Content, Data Extraction and Analysis, and Database Design,” In Protein Engineering. Protein Design in Basic Research, Medicine, and Industry (M. Ikehara, T. Oshima, and K. Titani, Eds.), Springer Verlag, New York, pp. 285290 (1990).

128. B. J. Stockman and J. L. Markley, “Methods of StableIsotopeAssisted Protein NMR Spectroscopy in Solution,” In Protein Structure and Engineering (O. Jardetzky, Ed.) Plenum Press, New York, pp. 155192 (1989).

129. J. Fejzo, W. M. Westler, S. Macura, and J. L. Markley, “Elimination of CrossRelaxation Effects from TwoDimensionalChemical Exchange Spectra of Macromolecules,” J. Am. Chem. Soc 112 25742577 (1990).

130. A. T. Alexandrescu, A. P. Hinck, and J. L. Markley, “Coupling Between Local Structure and Global Stability of a Protein: Mutants of Staphylococcal Nuclease,” Biochemistry 29, 45164525 (1990).

131. B.H. Oh and J. L. Markley, “Multinuclear Magnetic Resonance Studies of the 2Fe·2S* Ferredoxin from Anabaena species strain PCC 7120. 1. SequenceSpecific Hydrogen1 Resonance Assignments and Secondary Structure in Solution of the Oxidized Form,” Biochemistry 29, 39934004 (1990).

132. B.H. Oh, E. S. Mooberry, and J. L. Markley, “Multinuclear Magnetic Resonance Studies of the 2Fe·2S* Ferredoxin from Anabaena species strain PCC 7120. 2. SequenceSpecific Carbon13 and Nitrogen15 Resonance Assignments of the Oxidized Form,” Biochemistry 29, 40044011 (1990).

133. B.H. Oh and J. L. Markley, “Multinuclear Magnetic Resonance Studies of the 2Fe·2S* Ferredoxin from Anabaena species strain PCC 7120. 3. Detection and Characterization of HyperfineShifted Nitrogen15 and Hydrogen1 Resonances of the Oxidized Form,” Biochemistry 29, 40124017 (1990).

134. J. Wang, A. P. Hinck, S. N. Loh, and J. L. Markley, “TwoDimensional NMR Studies of Staphylococcal Nuclease: Evidence for Conformational Heterogeneity from Hydrogen1, Carbon13, and Nitrogen15 Spin System Assignments of the Aromatic Amino Acids in the Nuclease H124LThymidine 3',5'BisphosphateCa2+ Ternary Complex,” Biochemistry 29, 42424253 (1990).

135. Zs. Zolnai, S. Macura, and J. L. Markley, “Phasing Two and ThreeDimensional NMR Spectra by Use of the Hilbert Transform Can Save Computer Time and Space,” J. Magn. Reson. 89, 94101 (1990).

136. L. Skjeldal, W. M. Westler, and J. L. Markley, “Detection and Characterization of HyperfineShifted Resonances in the Proton Nuclear Magnetic Resonance Spectrum of Anabaena 7120 Ferredoxin at High Magnetic Fields,” Arch. Biochem. Biophys. 278, 482485 (1990).

137. Zs. Zolnai, W. M. Westler, E. L. Ulrich, and J. L. Markley, “Drafting Table and Light Box Software for Multidimensional NMR Spectral Analysis (PIXI). The Personal Computer Workstation,” J. Magn. Reson. 88, 511522 (1990).

138. K. E. Paulsen, M. T. Stankovich, B. J. Stockman, and J. L. Markley, “Redox and Spectral Properties of Flavodoxins from Anabaena 7120,” Arch. Biochem. Biophys. 280, 6873 (1990).

139. J. Alonso, C. Arús, W. M. Westler, and J. L. Markley, “TwoDimensional Spectra of Intact Tissue: Homonuclear HartmannHahn Spectroscopy Provides Increased Sensitivity and Information Content as Compared to COSY,” Magn. Reson. Med. 15, 142151 (1990).

140. A. P. Hinck, S. N. Loh, J. Wang, and J. L. Markley, “Histidine 121 of Staphylococcal Nuclease. Correction of the H2 1H NMR Assignment and Reinterpretation of the Role this Residue Plays in Conformational Heterogeneity of the Protein,” J. Am. Chem. Soc. 112, 90319034 (1990).

141. D. C. McCain and J. L. Markley, “In vivo Study of Chloroplast Volume Regulation,” Biophys. J. 61, 12071212 (1992).

142. D. C. McCain and J. L. Markley, “Distinguishing Chloroplast Water from Nonchloroplast Water in OneDimensional NMR Microscope Images of Plant Leaves,” J. Magn. Reson. 89, 410414 (1990).

143. B. J. Stockman, A. M. Krezel, J. L. Markley, K. G. Leonhardt, and N. A. Straus, “Hydrogen1, Carbon13, and Nitrogen15 NMR Spectroscopy of Anabaena 7120 Flavodoxin: Assignment of ßSheet and Flavin Binding Site Resonances and Analysis of ProteinFlavin Interactions,” Biochemistry 29 96009609 (1990).

144. J. Fejzo, W. M. Westler, S. Macura, and J. L. Markley, “Strategies for Eliminating Unwanted CrossRelaxation and CoherenceTransfer Effects from TwoDimensional ChemicalExchange Spectra,” J. Magn. Reson. 92, 2029 (1991).

145. J. L. Markley, P. Darba, J. Fejzo, A. M. Krezel, S. Macura, C. W. McNemar, E. S. Mooberry, B. R. Seavey, W. M. Westler, and Zs. Zolnai, “Computational Aspects of Multinuclear NMR Spectroscopy of Proteins at NMRFAM,” In Computational Aspects of the Study of Biological Macromolecules by Nuclear Magnetic Resonance Spectroscopy (J. C. Hoch, F. M. Poulsen, and C. Redfield, Eds.), NATO ASI Series, Plenum Press, New York, pp. 3950 (1991).

146. B. J. Stockman, A. M. Krezel, J. B. Olson, E. S. Mooberry, and J. L. Markley, “Flavin Binding Site Geometry in Anabaena 7120 Flavodoxin. Progress in Determining the Flavodoxin Solution Structure,” In Flavins and Flavoproteins 1990, (B. Curti, S. Ronchi, and G. Zanetti, Eds.) Walter de Gruyter, Berlin, pp. 377380 (1991).

147. A. S. Edison, W. M. Westler, and J. L. Markley, “Elucidation of Protein Spin Systems and Determination of Heteronuclear Coupling Constants by CarbonProtonProton ThreeDimensional NMR,” J. Magn. Reson. 92, 434438 (1991).

148. S. N. Loh, C. W. McNemar, and J. L. Markley, “Detection and Kinetic Characterization of a Novel Proline Isomerism in Staphylococcal Nuclease by NMR Spectroscopy,” In Techniques in Protein Chemistry II, (J. J. Villafranca, Ed.), Academic Press, New York, pp. 275282 (1991).

149. J. Fejzo, W. M. Westler, S. Macura, and J. L. Markley, “Elimination of ChemicalExchangeMediated Spin Diffusion from Exchange Spectra of Macromolecules. ExchangeDecoupled NOESY (XDNOESY),” J. Magn. Reson. 92, 195202 (1991).

150. W. R. Rypniewski, D. R. Breiter, M. M. Benning G. Wesenberg, B.H. Oh, J. L. Markley, I. Rayment, and H. M. Holden, “Crystallization and Structure Determination to 2.5 Å Resolution of the Oxidized [2Fe2S] Ferredoxin Isolated from Anabaena 7120,” Biochemistry 30, 41264131 (1991).

151a. B. R. Seavey, E. A. Farr, W. M. Westler, and J. L. Markley, “A Relational Database for SequenceSpecific Protein NMR Data,” J. Biomol. NMR 1, 217230 (1991).

151b. J. L. Markley, E. A. Farr, and B. R. Seavey, “Appendix: Check List for Protein NMR Data to be Submitted for Publication or for Database Inclusion,” J. Biomol. NMR 1, 231236 (1991).

152. D. C. McCain, W. M. Westler, and J. L. Markley, “A TwoDimensional Technique for Chemical Shift Resolution in OneDimensional NMR Images,” J. Magn. Reson. 93, 181183 (1991).

153. J. Fejzo, A. M. Krezel, W. M. Westler, S. Macura, and J. L. Markley, “Direct CrossRelaxation NOESY (D.NOESY). A Method for Removing SpinDiffusion Cross Peaks from TwoDimensional NOE Spectra of Macromolecules,” J. Magn. Reson. 92, 651657 (1991).

154. J. Fejzo, A. M. Krezel, W. M. Westler, S. Macura and J. L. Markley, “Refinement of the NMR Solution Structure of a Protein to Remove Distortions Arising from Neglect of Internal Motion,” Biochemistry 30, 38073811 (1991).

155. J. L. Markley, “StableIsotopeAssisted Multinuclear NMR Investigations of Proteins,” In ProteinsStructure, Dynamics and Design, (V. Renugopalakrishnan, P. R. Carey, I. C. P. Smith, S.G. Huang, and A. C. Storer, Eds.), ESCOM, Leiden, pp. 2939 (1991).

156. L. Skjeldal, W. M. Westler, B.H. Oh, A. M. Krezel, H. M. Holden, B. L. Jacobson, I. Rayment, and J. L. Markley, “TwoDimensional Magnetization Exchange Spectroscopy of Anabaena 7120 Ferredoxin. Nuclear Overhauser Effect and Electron SelfExchange Cross Peaks from Amino acid Residues Surrounding the 2Fe2S* Cluster,” Biochemistry 30, 73637368 (1991).

157. S. Kornguth, E. Bersu, M. E. Anderson, and J. L. Markley, “Correlation of Increased Levels of Class I MHC H2Kk in the Placenta of Murine Trisomy 16 Conceptuses with Structural Abnormalities Revealed by Magnetic Resonance Microscopy,” Tetralogy 45, 383391 (1992).

158. L. Skjeldal, J. L. Markley, V. M. Coghlan, and L. E. Vickery, “1H NMR Spectra of Vertebrate [2Fe2S] Ferredoxins. Hyperfine Resonances Suggest Different Electron Delocalization Patterns from Plant Ferredoxins,” Biochemistry 30, 90789083 (1991).

159. J. Wang, E. S. Mooberry, W. F. Walkenhorst, and J. L. Markley, “Solution Studies of Staphylococcal Nuclease H124L. 1. Backbone 1H and 15N Resonances and Secondary Structure of the Unligated Enzyme as Identified by ThreeDimensional NMR Spectroscopy,” Biochemistry 31, 911920 (1992).

160. J. Wang, A. P. Hinck, S. N. Loh, D. M. LeMaster, and J. L. Markley, “Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes that Accompany Formation of the NucleaseThymidine3',5' BisphosphateCalcium Ternary Complex,” Biochemistry 31, 921936 (1992).

161. D. C. McCain and J. L. Markley, “A Nuclear Magnetic Resonance Imaging Technique Designed for Studies of Water in Plant Leaves,” J. Struct. Biol. 108, 195201 (1992).

162. A. L. P. Houseman, B.H. Oh, M. C. Kennedy, C. Fan, M. M. Werst, H. Beinert, J. L. Markley, and B. M. Hoffman, “14,15N, 13C, 57Fe, 1,2H Qband ENDOR Study of FeS Proteins with Clusters that Have Endogenous Sulfur Ligands,” Biochemistry 31, 20732080 (1992).

163. J. Fejzo, W. M. Westler, J. L. Markley, S. Macura, “Complete Elimination of Spin Diffusion from Selected Resonances in TwoDimensional CrossRelaxation Spectra of Macromolecules by a Novel Pulse Sequence (SNOESY),” J. Am. Chem. Soc. 114, 15231524 (1992).

164. B. L. Jacobson, Y. K. Chae, H. Böhme, J. L. Markley, and H. M. Holden, “Crystallization and Preliminary Analysis of Oxidized, Recombinant, Heterocyst [2Fe2S] Ferredoxin from Anabaena 7120,” Arch. Biochem. Biophys. 294, 279281 (1992).

165. Ž. Džakula, W. M. Westler, A. S. Edison and J. L. Markley, “The “CUPID” Method for Calculating the Continuous Probability Distribution of Rotamers from NMR Data,” J. Am. Chem. Soc. 114, 61956199 (1992).

166. Ž. Džakula, A. S. Edison, W. M. Westler, and J. L. Markley, “Analysis of χ1 Rotamer Populations from NMR Data by the CUPID Method,” J. Am. Chem. Soc. 114, 62006207 (1992).

167. B. J. Stockman and J. L. Markley, “NMR Analysis of Ligand Binding,” Current Opinion Structural Biology 2, 5256 (1992).

168. S. Macura, J. Fejzo, C. G. Hoogstraten, W. M. Westler, and J. L. Markley, “Topological Editing of CrossRelaxation Networks,” Israel J. Chem. 32, 245256 (1992).

169. S. T. Rao, F. Shaffie, C. Yu, K. A. Satyshur, B. J. Stockman, J. L. Markley, and M. Sundaralingam, “Structure of the Oxidized LongChain Flavodoxin from Anabaena 7120 at 2 Å Resolution,” Protein Science 1, 14131427 (1992).

170. D. D. Gilboe, D. Kintner, M. E. Anderson, J. H. Fitzpatrick, S. E. Emoto, and J. L. Markley, “Inorganic Phosphate Compartmentation in the Normal Isolated Canine Brain,” J. Neurochem. 60, 21922203 (1993).

171. C. Royer, A. P. Hinck, S. N. Loh, K. Prehoda, X. Peng, J. Jonas, and J. L. Markley, “Effects of Amino Acid Substitutions on the Pressure Denaturation of Staphylococcal Nuclease as Monitored by Fluorescence and Nuclear Magnetic Resonance Spectroscopy,” Biochemistry 32, 52225232 (1993).

172. E. S. Mooberry, A. S. Edison, F. Abildgaard, J. L. Markley, I.J. L. Byeon, and M.D. Tsai, “Modification of a Bruker AM600 Spectrometer for Double and Triple Resonance Three and FourDimensional Experiments Illustrated with Chicken Adenylate Kinase Resonance Assignments,” In Spectroscopy and Structure of Molecules and Nuclei, (N. R. Johnson, W. N. Shelton, and M. ElSayed, Eds.), World Scientific, Singapore, pp. 375380 (1992).

173. M. E. Anderson, J. L. Markley, C. Arùs, and M. C. Chobanian, “A Perifusion LoopGap Resonator NMR Probe for Aerobic Cell Suspensions,” Magn. Reson. Med. 29, 563566 (1993).

174. A. P. Hinck, W. F. Walkenhorst, W. M. Westler, S. Choe, and J. L. Markley, “Overexpression and Purification of Avian Ovomucoid Third Domains in Escherichia coli,” Protein Eng. 6, 221227 (1993).

175. S. N. Loh and J. L. Markley, “Measurement of Amide Hydrogen D/H Fractionation Factors in Proteins by NMR Spectroscopy,” In Techniques in Protein Chemistry IV, (R. Angeletti, Ed.), Academic Press, New York, pp. 517524 (1993).

176. J. L. Markley and M. Kainosho, “Stable Isotope Labeling and Resonance Assignments in Larger Proteins,” In NMR of Biological Macromolecules: A Practical Approach, (G. C. K. Roberts, Ed.), Oxford University Press, Oxford, pp. 101152 (1993).

177. R. Chylla and J. L. Markley, “Simultaneous Basepoint Correction and Signal Recognition in Multidimensional NMR Spectra,” J. Magn. Reson., Series B 102, 148154 (1993).

178. D. C. McCain, J. Croxdale, and J. L. Markley, “Spatial Distribution of Chloroplast Water in Acer platanoides Sun and Shade Leaves,” Plant Cell and Environment 16, 727733 (1993).

179. S. Macura, W. M. Westler, and J. L. Markley, “TwoDimensional Exchange Spectroscopy of Proteins,” Methods Enzymol. 239 106144 (1994).

180. B. L. Jacobson, Y. K. Chae, J. L. Markley, I. Rayment, and H. M. Holden, “Molecular Structure of the Oxidized, Recombinant, Heterocyst [2Fe2S] Ferredoxin from Anabaena 7120 Determined to 1.7 Å Resolution,” Biochemistry 32, 67886793 (1993).

181a. J. L. Markley, A. P. Hinck, S. N. Loh, K. Prehoda, D. Truckses, W. F. Walkenhorst, and J. Wang, “Case Study of Protein Structure, Stability, and Function: NMR Investigations of the Proline Residues in Staphylococcal Nuclease,” Pure & Appl. Chem. 66, 6569 (1994).

181b. J. L. Markley, A. P. Hinck, S. N. Loh, K. Prehoda, D. Truckses, W. F. Walkenhorst, and J. Wang, “Case Study of Protein Structure, Stability, and Function: NMR Investigations of the Proline Residues in Staphylococcal Nuclease,” In Protein Structure Function Relationship (Z. H. Zaidi, A. Abbasi, and D. L. Smith, Eds.), TWEL Publishers, KarachiDoncasterGaithersburg, pp. 193202 (1993).

182. A. S. Edison, J. L. Markley, and F. Weinhold, “Calculations of Nuclear SpinSpin Coupling Constants with Ab Initio Molecular Orbital Wave Functions,” J. Phys. Chem. 97, 1165711665 (1993).

183. M. E. Cabañas, J. Alonso, C. Arús, M. E. Anderson, W. M. Westler, and J. L. Markley, “A Versatile Perifusion System for the NMR Spectroscopy of Bovine Retina. Assignment of Resonances and Effect of Ischemia,” Exp Eye Res., 57 669678 (1993).

184. A. P. Hinck, E. S. Eberhardt, and J. L. Markley, “NMR Strategy for Elucidation of XaaPro Peptide Bond Configurations in Proteins: Mutants of Staphylococcal Nuclease with Altered Configuration at Proline117,” Biochemistry 32, 1181011818 (1993).

185. R. A. Chylla, and J. L. Markley, “Improved Frequency Resolution in Multidimensional ConstantTime Experiments by Multidimensional Bayesian Analysis,” J. Biomol. NMR 3, 515533 (1993).

186. J. K. Hurley, Z. Salamon, T. E. Meyer, J. C. Fitch, M. A. Cusanovich, J. L. Markley, H. Cheng, B. Xia, Y. K. Chae, M. Medina, C. GómezMoreno, and G. Tollin, “Amino Acid Residues in Anabaena Ferredoxin Crucial to Interaction with FerredoxinNADP+ Reductase: SiteDirected Mutagenesis and Laser Flash Photolysis,” Biochemistry 32, 93469354 (1993).

187. S. N. Loh, K. E. Prehoda, J. Wang, and J. L. Markley, “Hydrogen Exchange in Unligated and Ligated Staphylococcal Nuclease,” Biochemistry 32, 1102211028 (1993).

188. S. N. Loh, and J. L. Markley, “Hydrogen Bonding in Proteins as Studied by Amide Hydrogen D/H Fractionation Factors: Application to Staphylococcal Nuclease,” Biochemistry 33, 10291036 (1994).

189. J. B. Olson, Jr., and J. L. Markley, “Evaluation of an Algorithm for the Automated Sequential Assignment of Protein Backbone Resonances: A Demonstration of the Connectivity Tracing Assignment Tools (CONTRAST) Software Package,” J. Biomol. NMR 4, 385410 (1994).

190. C. G. Hoogstraten, W. M. Westler, S. Macura, and J. L. Markley, “Improved Measurement of Longer ProtonProton Distances in Proteins by Relaxation Network Editing,” J. Magn. Reson., Series B, 102, 232235 (1993).

191. A. S. Edison, J. L. Markley, and F. Weinhold, “Calculations of One, Two and ThreeBond Nuclear SpinSpin Couplings in a Model Peptide and Correlations with Experimental Data,” J. Biomol. NMR 4, 519542 (1994).

192. A. S. Edison, F. Weinhold, W. M. Westler, and J. L. Markley, “Estimates of and Torsion Angles in Proteins from One, Two and ThreeBond Nuclear SpinSpin Couplings: Application to Staphylococcal Nuclease,” J. Biomol. NMR 4, 543551 (1994).

193. A. M. Krezel, P. Darba, A. D. Robertson, J. Fejzo, S. Macura, and J. L. Markley, “Solution Structure of Turkey Ovomucoid Third Domain as Determined from Nuclear Magnetic Resonance Data,” J. Mol. Biol. 242, 203214 (1994).

194. W. F. Walkenhorst, A. M. Krezel, G. I. Rhyu, and J. L. Markley, “Solution Structure of ReactiveSite Hydrolyzed Turkey Ovomucoid Third Domain by Nuclear Magnetic Resonance and Distance Geometry Methods,” J. Mol. Biol. 242, 215230 (1994).

195. A. S. Edison, F. Abildgaard, W. M. Westler, E. S. Mooberry, and J. L. Markley, “Practical Introduction to the Theory and Implementation of Multinuclear, Multidimensional Nuclear Magnetic Resonance Experiments,” Methods. Enzymol. 239, 379 (1994).

196. E. S. Mooberry, F. Abildgaard, and J. L. Markley, “Modifications of Older Model Nuclear Magnetic Resonance Console for Collection of Multinuclear, Multidimensional Spectral Data,” Methods. Enzymol. 239, 247256 (1994).

197. S. Macura, J. Fejzo, W. M. Westler, and J. L. Markley, “Influence of Slow Internal Motion in Proteins on CrossRelaxation Rates Determined by TwoDimensional Exchange Spectroscopy,” Bull. Magn. Reson. 16, 7393 (1994). RR02301, NMRFAM instrumentation

198. J. K. Hurley, H. Cheng, B. Xia, J. L. Markley, M. Medina, C. GómezMoreno, and G. Tollin, “An Aromatic Amino Acid is Required at Position 65 in Anabaena Ferredoxin for Rapid Electron Transfer to Ferredoxin:NADP+ Reductase,” J. Am. Chem. Soc. 115 1169811701 (1993).

199. H. Zhao, W. M. Westler and J. L. Markley, “Precise Determination of T1 Relaxation Values by a Method in which Pairs of Nonequilibrium Magnetizations are Measured across a Constant Relaxation Period,” J. Magn. Reson. Ser. A 112, 139143 (1995).

200. Y. K. Chae, F. Abildgaard, E. S. Mooberry, and J. L. Markley, “Multinuclear, Multidimensional NMR Studies of Anabaena 7120 Heterocyst Ferredoxin. SequenceSpecific Resonance Assignments and Secondary Structure of the Oxidized Form in Solution,” Biochemistry 33, 32873295 (1994).

201. H. M. Holden, B. L. Jacobson, J. K. Hurley, G. Tollin, B.H. Oh, L. Skjeldal, Y. K. Chae, H. Cheng, B. Xia, and J. L. Markley, “StructureFunction Studies of [2Fe2S] Ferredoxins,” J. Bioeng. Biomemb. 26, 6788 (1994).

202. I.J. L. Byeon, H. Yan, A. S. Edison, E. S. Mooberry, F. Abildgaard, J. L. Markley, and M.D. Tsai, “Mechanism of Adenylate Kinase. 1H, 13C, and 15N NMR Assignments, Secondary Structure, and Substrate Binding Sites,” Biochemistry 32, 1250812521 (1993).

203. Y. K. Chae and J. L. Markley, “Analysis of the HyperfineShifted Nitrogen15 Resonances of the Oxidized Form of Anabaena 7120 Heterocyst Ferredoxin,” Biochemistry 34, 188193 (1995).

204. H. Cheng, B. Xia, G. H. Reed, and J. L. Markley, “Optical, EPR, and 1H NMR Spectroscopy of SerineLigated [2Fe2S] Ferredoxins Produced by SiteDirected Mutagenesis of Cysteine Residues in Recombinant Anabaena 7120 Vegetative Ferredoxin,” Biochemistry, 33 31553164 (1994).

205. J. K. Hurley, Z. Salamon, T. E. Meyer, J. C. Fitch, M. A. Cusanovich, G. Tollin, H. Cheng, B. Xia, Y. K. Chae, J. L. Markley, M. Medina, and C. GómezMoreno, “StructureFunction Relationships in Ferredoxin: SiteDirected Mutagenesis and TimeResolved Absorption Spectroscopy Applied to the Ferredoxin:Ferredoxin NADP+ Reductase Interaction,” In Flavins and Flavoproteins 1993 (K. Yagi, Ed.), Walter de Gruyter, Berlin, pp. 435438 (1994).

206. S. Kornguth, M. Anderson, J. L. Markley, and A. Shedlovsky, “NearMicroscopic Magnetic Resonance Imaging of the Brains of Phenylalanine HydroxylaseDeficient Mice, Normal Littermates, and of Normal BALB/c Mice at 9.4 Tesla,” Neuroimage 1, 220229 (1994).

207. M. Ghassemian, B. Wong, F. Ferreira, J. L. Markley, and N. Straus, “Cloning, Sequencing and Transcriptional Studies of the Genes for Cytochrome c553 and Plastocyanin from Anabaena sp. PCC 7120,” Microbiology 140, 11511159 (1994).

208. S. N. Loh, K. E. Prehoda, J. Wang, and J. L. Markley, “Measuring Global and Local Structural Free Energy Changes in Staphylococcal Nuclease by NMRObserved Hydrogen Exchange,” In Techniques in Protein Chemistry V (J. W. Crabb, Ed.), Academic Press, New York, pp. 431438 (1994).

209. B. M. Burkhart, B. Ramakrishnan, H. Yan, R. J. Reedstrom, J. L. Markley, N. A. Straus, and M. Sundaralingam, “Structure of the Trigonal Form of Recombinant Oxidized Flavodoxin from Anabaena 7120 at 1.40 Å Resolution,” Acta. Crystallogr. Ser. D. 51, 318330 (1995).

210. Y. K. Chae, B. Xia, H. Cheng, B.H. Oh, L. Skjeldal, W. M. Westler, and J. L. Markley, “Multinuclear Magnetic Resonance and Mutagenesis Studies of StructureFunction Relationships in [2Fe2S] Ferredoxins,” In Nuclear Magnetic Resonance of Paramagnetic Proteins (G. N., LaMar, Ed.), Nato ASI Series C, Vol. 457, Kluwer, Dordrecht, pp. 297317 (1995).

211. H. Cheng, B. Xia, Y. K. Chae, W. M. Westler, and J. L. Markley, “Magnetic Resonance Studies of Isotopically Labeled Paramagnetic Proteins: [2Fe2S] Ferredoxins,” In Stable Isotope Applications in Biomolecular Structure and Mechanisms (J. Trewhella, T. Cross, & C. J. Unkefer, Eds.), Los Alamos National Laboratory, Los Alamos, pp. 171188 (1994).

212. B. Xia, H. Cheng, L. Skjeldal, V. M. Coghlin, L. E. Vickery, and J. L. Markley, “Multinuclear Magnetic Resonance and Mutagenesis Studies of the Histidine Residues of Human Mitochondrial Ferredoxin,” Biochemistry 34, 180187 (1995).

213. H. Cheng, W. M. Westler, B. Xia, B.H. Oh, and J. L. Markley, “Protein Expression, Selective Isotopic Labeling, and Analysis of HyperfineShifted NMR Signals of Anabaena 7120 Vegetative [2Fe2S] Ferredoxin,” Arch. Biochem. Biophys 316, 619634 (1995).

214. H. Cheng and J. L. Markley, “NMR Spectroscopic Studies of Paramagnetic Proteins: IronSulfur Proteins,” Ann. Rev. Biophys. Biomol. Structure 24, 209237 (1995).

215. K. E. Prehoda and J. L. Markley, “Use of Partial Molar Volumes of Model Compounds in the Interpretation of HighPressure Effects on Proteins,” In HighPressure Effects in Molecular Biophysics and Enzymology (J. L. Markley, C. A. Royer, and D. Northrop, Eds.), Oxford University Press, pp. 3343 (1996).

216. R. A. Chylla and J. L. Markley, “Theory and Application of the Maximum Likelihood Principle to NMR Parameter Estimation of Multidimensional NMR Data,” J. Biomol. NMR 5, 245258 (1995).

217. J. K. Hurley, M. S. Caffrey, J. L. Markley, H. Cheng, B. Xia, Y. K. Chae, H. M. Holden, and G. Tollin, “Mutations of Surface Residues in Anabaena Vegetative and Heterocyst Ferredoxin that Affect Thermodynamic Stability as Determined by Guanidine Hydrochloride Denaturation,” Protein Sci. 4, 5864 (1995).

218. C. GómezMoreno, M. Medina, J. K. Hurley, M. A. Cusanovich, J. L. Markley, H. Cheng, B. Xia, Y. K. Chae, and G. Tollin, “Protein Engineering for the Elucidation of the Mechanism of Electron Transfer in Redox Proteins,” Biochem. Soc. Trans. 22, 796800 (1994).

219. J. Haginaka, T. Murashima, T. C., Pinkerton, J. P. Comiskey, E. L. Ulrich, J. L. Markley, and W. F. Walkenhorst, “Enantioselectivity of Ovomucoid BondedPhase HPLC Columns Produced with Isolated Domains,” Kuromatogurafi 14, 100101 (1993).

220. J. B. Pearson, J.F. Wang, J. L. Markley, H.b. Le, and E. Oldfield, “Protein Structure Refinement Using Carbon13 Nuclear Magnetic Resonance Spectroscopic Chemical Shifts and Quantum Chemistry,” J. Am. Chem. Soc. 117, 88238829 (1995).

221. Zs. Zolnai, N. Juranić, J. L. Markley, and S. Macura, “Magnetization Exchange Network Editing: Mathematical Principles and Experimental Demonstration,” Chem. Phys. 200, 161179 (1995).

222. G. J. A. Vidugiris, J. L. Markley, and C. A. Royer, “Evidence for a Molten GlobuleLike Transition State in Protein Folding from Determination of Activation Volumes,” Biochemistry 34, 49094912 (1995).

223. C. G. Hoogstraten, W. M. Westler, E. S. Mooberry, S. Macura, and J. L. Markley, “Analysis of Transverse Cross Relaxation in Proteins within a Simplified Relaxation Submatrix: BDROESY,” J. Magn. Reson. Ser. B 109, 7679 (1995).

224. T. C. Pinkerton, W. J. Howe, E. L. Ulrich, J. P. Comiskey, J. Haginaka, T. Murashima, W. F. Walkenhorst, W. M. Westler, and J. L. Markley, “Protein Binding Chiral Discrimination of HPLC Stationary Phases made with Whole, Fragmented, and Third Domain Turkey Ovomucoid,” Anal. Chem. 67, 23542367 (1995).

225. A. S. Edison, F. Weinhold, and J. L. Markley, “Theoretical Studies of Protium/Deuterium Fractionation Factors and Cooperative Hydrogen Bonding in Peptides,” J. Am. Chem. Soc. 117, 96199624 (1995).

226. A. S. Edison, J. L. Markley, and F. Weinhold, “Ab Initio Calculations of Protium/Deuterium Fractionation Factors in O2H5+ Clusters,” J. Phys. Chem. 99, 80138016 (1995).

227. D. Ming, J. L. Markley, and G. Hellekant, “Quantification of Cysteinyl Sulfhydryl Residues in Peptides and Proteins by ESIMS or MALDIMS,” BioTechniques 18, 808810 (1995).

228. J. Schleucher, J. L. Markley, and T. D. Sharkey, “Hydrogen Isotope Ratios of Plant Metabolites,” In Photosynthesis: from Light to Biosphere (P. Mathis, Ed.), Kluwer Academic Publishers, Vol. V, pp. 10091012 (1995).

229. D. S. Wishart, C. G. Bigam, J. Yao, F. Abildgaard, H. J. Dyson, E. Oldfield, J. L. Markley, and B. D. Sykes, “1H 13C and 15N Chemical Shift Referencing in Biomolecular NMR,” J. Biomol. NMR 6, 135140 (1995).

230. B. Xia, W. M. Westler, H. Cheng, J. Meyer, J.M. Moulis, and J. L. Markley, “Detection and Classification of Hyperfineshifted 1H, 2H, and 15N Resonances from the Four Cysteines that Ligate Iron in Oxidized and Reduced Clostridium pasteurianum Rubredoxin,” J. Am. Chem. Soc. 117, 53475350 (1995).

231. C. G. Hoogstraten, W. M. Westler, S. Macura, and J. L. Markley, “NOE Measurements in the Absence of Spin Diffusion: Application to Methylene Groups in Proteins and Effects on Local Structural Parameters,” J. Am. Chem. Soc. 117, 56105611 (1995); correction, loc. cit. p. 8885.

232. J. A. Navarro, M. Hervás, C. Genzor, G. Cheddar, M. F. Fillat, M. A. de la Rosa, C. GómezMoreno, H. Cheng, B. Xia, Y. K. Chae, H. Yan, B. Wong, N. Straus, J. L. Markley, J. K. Hurley, and G. Tollin, “SiteSpecific Mutagenesis Demonstrates that the Structural Requirements for Efficient Electron Transfer in Anabaena Ferredoxin and Flavodoxin are Highly Dependent on the Reaction Partner: Kinetic Studies with Photosystem I, Ferredoxin:NADP+ Reductase and Cytochrome c,” Arch. Biochem. Biophys. 321, 229238 (1995).

233. C. G. Hoogstraten, S. Choe, W. M. Westler, and J. L. Markley, “Comparison of the Accuracy of Protein Solution Structures Derived from Conventional and NetworkEdited NOESY Data,” Protein Science 4, 22892299 (1995).

234. B. Xia, H. Cheng, Y. K. Chae, L. Skjeldal, W. M. Westler, and J. L. Markley, “IronSulfur Proteins: Investigations of HyperfineShifted Hydrogen, Carbon, and Nitrogen Resonances,” In NMR as a Structural Tool For Macromolecules: Current Status and Future Directions (B. D. Nageswara Rao and M. D. Kemple, Eds.), Plenum Press, pp. 251274 (1996).

235. J. L. Markley, B. Xia, Y. K. Chae, H. Cheng, W. M. Westler, J. D. Pikus, and B. G. Fox, “NMR Approaches to the Study of StructureFunction Relationships in IronSulfur Proteins: Rubredoxin, [2Fe2S] Ferredoxins, and a Rieske Protein,” In Protein Structure Function Relationship (Z. H. Zaidi and D. L. Smith, Eds.), Plenum Press, London, pp. 135146 (1996).

236. Ž. Džakula, W. M. Westler, and J. L. Markley, “Continuous Probability Distribution (CUPID) Analysis of Potentials for Internal Rotations,” J. Magn. Reson. Ser B 111, 109126 (1996).

237. Y. K. Chae and J. L. Markley, “Mutagenesis Studies of Anabaena 7120 [2Fe2S] Ferredoxins: Physical and Chemical Characteristics of Hybrid Vegetative/Heterocyst Sequences,” In Photosynthesis: from Light to Biosphere (P. Mathis, Ed.), Kluwer Academic Publishers, Vol. II, pp. 633638 (1995).

238. A. P. Hinck, W. F. Walkenhorst, D. Truckses, and J. L. Markley, “NMR and Mutagenesis Investigations of a Model Cis:Trans Peptide Isomerization Reaction: Xaa116Pro117 of Staphylococcal Nuclease and its Role in Protein Stability and Folding,” In Biological NMR Spectroscopy (J. L. Markley and S. J. Opella, Eds.), Oxford University Press, New York pp. 113138 (1996).

239. Zs. Zolnai, N. Juranić, J. L. Markley, and S. Macura, “Zooming, a Practical Strategy for Improving the Quality of Multidimensional NMR Spectra,” J. Magn. Reson. Ser. A. 119, 5364 (1996).

240. K. E. Prehoda, S. N. Loh, and J. L. Markley, “Modeling Volume Changes in Proteins using Partial Molar Volumes of Model Compounds,” In Techniques in Protein Chemistry VII (D. R. Marshak, Ed.), Academic Press, New York, pp. 433438 (1996).

241. G. J. A. Vidugiris, D. M. Truckses, J. L. Markley, and C. A. Royer, “HighPressure Denaturation of Staphylococcal Nuclease ProlinetoGlycine Substitution Mutants,” Biochemistry 35, 38573864 (1996).

242. J. L. Markley and W. M. Westler, “ProtonationState Dependence of Hydrogen Bond Strengths and Exchange Rates in a Serine Protease Catalytic Triad: Bovine Chymotrypsinogen A,” Biochemistry 35, 1109211097 (1996).

243. C. B. Hoogstraten and J. L. Markley, “Approaches to the Determination of More Accurate CrossRelaxation Rates and the Effects of Improved Distance Constraints on Protein Solution Structures,” In Dynamics and the Problem of Recognition in Biological Macromolecules (O. Jardetzky and J.F. Lefvre, Eds.), Plenum Press, New York, pp. 73111 (1996).

244. C. G. Hoogstraten and J. L. Markley, “Effects of Experimentally Achievable Improvements in the Quality of NMR Distance Constraints on the Accuracy of Calculated Protein Structures,” J. Mol. Biol. 258, 334348 (1996).

245. D. M. Truckses, J. R. Somoza, K. E. Prehoda, S. C. Miller, and J. L. Markley, “Coupling between trans/cis Proline Isomerization and Protein Stability in Staphylococcal Nuclease,” Protein Sci. 5, 19071916 (1996).

246. A. P. Hinck, D. M. Truckses, and J. L. Markley, “Engineered Disulfide Bonds in Staphylococcal Nuclease: Effects on the Stability and Conformation of the Folded Protein,” Biochemistry 35, 1032810338 (1996).

247. B. Xia, H. Cheng, V. Bandarian, G. H. Reed, and J. L. Markley, “Human Ferredoxin: Overproduction in Escherichia coli, Reconstitution in vitro, and Spectroscopic Studies of IronSulfur Cluster Ligand CysteinetoSerine Mutants,” Biochemistry 35, 94889495 (1996).

248. Ž. Džakula, M. L. DeRider, and J. L. Markley, “Conformational Analysis of Molecules with FiveMembered Rings through NMR Determination of the Continuous Probability Distribution (CUPID) for Pseudorotation,” J. Am. Chem. Soc. 118, 1279612803 (1996).

249. H. Rémigy, M. Jaquinod, Y. Pétillot, J. Gagnon, H. Cheng, B. Xia, J. L. Markley, J. K. Hurley, G. Tollin, and E. Forest, “Probing the Influence of Mutations on the Stability of a Ferredoxin by Mass Spectrometry,” J. Protein Chem. 16, 527532 (1997).

250. G. Kaslik, J. Kardos, E. Szabó, L. Szilágyi, P. Závodszky, W. M. Westler, J. L. Markley, and L. Gráf, “Effects of Serpin Binding on the Target Proteinase: Global Stabilization, Localized Increased Structural Flexibility, and Conserved Hydrogen Bonding at the Active Site,” Biochemistry 29, 54555464 (1997).

251. J. Wang, D. M. Truckses, F. Abildgaard, Ž. Džakula, Zs. Zolnai, and J. L. Markley, “Solution Structures of Staphylococcal Nuclease from Multidimensional Multinuclear NMR: NucleaseH124L and its Ternary Complex with Ca2+ and Thymidine3',5'Bisphosphate,” J. Biomol. NMR 10, 143164 (1997).

252. P. T. Chivers, K. E. Prehoda, B. F. Volkman, B.M. Kim, J. L. Markley, and R. T. Raines, “Microscopic pKa Values of Escherichia coli Thioredoxin,” Biochemistry 36, 1498514991 (1997).

253. Z. An, Q. Zhao, J. McEvoy, W. M. Yuan, J. L. Markley, and S. A. Leong, “The Second Finger of Urbs1 is Required for IronMediated Repression of sid1 in Ustilago maydis,” Proc. Natl. Acad. Sci. USA 94, 58825887 (1997).

254a. J. L. Markley, A. Bax, Y. Arata, C. W. Hilbers, R. Kaptein, B. D. Sykes, P. E. Wright, and K. Wüthrich, “Recommendations for the Presentation of NMR Structures of Proteins and Nucleic Acids (IUPAC Recommendations 1998),” Pure & Appl. Chem. 70, 117142 (1998).

254b. J. L. Markley, A. Bax, Y. Arata, C. W. Hilbers, R. Kaptein, B. D. Sykes, P. E. Wright, and K. Wüthrich, “Recommendations for the Presentation of NMR Structures of Proteins and Nucleic Acids: IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy,” J. Biomol. NMR 12, 123 (1998).

254c. J. L. Markley, A. Bax, Y. Arata, C. W. Hilbers, R. Kaptein, B. D. Sykes, P. E. Wright, and K. Wüthrich, “Recommendations for the Presentation of NMR Structures of Proteins and Nucleic Acids,” J. Mol. Biol. 280, 933952 (1998).

254d. J. L. Markley, A. Bax, Y. Arata, C. W. Hilbers, R. Kaptein, B. D. Sykes, P. E. Wright, and K. Wüthrich, “Recommendations for the Presentation of NMR Structures of Proteins and Nucleic Acids: IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy,” Eur. J. Biochem. 256, 115 (1998).

255a. J. K. Hurley, A. M. WeberMain, M. T. Stankovich, M. M. Benning, J. B. Thoden, J. L. Vanhooke, H. M. Holden, Y. K. Chae, B. Xia, H. Cheng, J. L. Markley, M. MartinezJúlvez, C. GómezMoreno, J. L. Schmeits, and G. Tollin, “StructureFunction Relationships in Anabaena Ferredoxin: Correlations Between Xray Crystal Structures, Reduction Potentials, and Rate Constants of Electron Transfer to Ferredoxin:NADP+ Reductase for SiteSpecific Ferredoxin Mutants,” Biochemistry 36, 1110011117 (1997).

255b. S. A. Leong, Z. An, G. Gentil, Q. Zhao, W. Yuan, M. Warriner, A. Budde, J. L. Markley, and H. von Döhren, “Organization and Regulation of a Siderophore Gene Cluster in Ustilago maydis,” In Developments in Industrial Microbiology- GMBIM (R. H. Baltz, G. D. Hegeman and P. L. Skatrud, Eds.), Society for Industrial Biology, pp. 8991 (1997).

256. S. L. Alam, B. F. Volkman, J. L. Markley, and J. D. Satterlee, “Detailed NMR Analysis of the HemeProtein Interactions in Component IV Glycera dibranchiata Monomeric HemoglobinCO,” J. Biomol. NMR 11, 119133 (1998).

257. B. F. Volkman, A. M. Prantner, S. J. Wilkens, B. Xia, and J. L. Markley, “Assignment of 1H, 13C, and 15N Signals of Oxidized Clostridium pasteurianum Rubredoxin,” J. Biomol. NMR 10, 409410 (1997).

258. J. Caldwell and J. L. Markley, “StructureFunction Relationships in SweetTasting Proteins,” Jour. Chem. Soc. Pakistan 21, 268280 (1999).

259. J. K. Hurley, A. M. WeberMain, A. E. Hodges, M. T. Stankovich, M. M. Benning, H. M. Holden, H. Cheng, B. Xia, J. L. Markley, C. Genzor, C. GómezMoreno, R. Hafezi, and G. Tollin, “IronSulfur Cluster CysteinetoSerine Mutants of Anabaena [2Fe2S] Ferredoxin Exhibit Unexpected Redox Properties and are Competent in Electron Transfer to Ferredoxin:NADP+ Reductase,” Biochemistry 36, 1510915117 (1997).

260. A. M. WeberMain, J. K. Hurley, H. Cheng, B. Xia, Y. K. Chae, J. L. Markley, M. MartinezJúlvez, C. GómezMoreno, M. T. Stankovich, and G. Tollin, “An Electrochemical, Kinetic, and Spectroscopic Characterization of [2Fe2S] Vegetative and Heterocyst Ferredoxins from Anabaena 7120 with Mutations in the Cluster Binding Loop,” Arch. Biochem. Biophys. 355, 181188 (1998).

261. S. J. Wilkens, B. Xia, F. Weinhold, J. L. Markley, and W. M. Westler, “NMR Investigations of Clostridium pasteurianum Rubredoxin. Origin of Hyperfine 1H, 2H, 13C, and 15N NMR Chemical Shifts in IronSulfur Proteins as Determined by Comparison of Experimental Data with Hybrid Density Functional Calculations,” J. Am. Chem. Soc. 120, 48064814 (1998).

262. R. Chylla, B. F. Volkman, and J. L. Markley, “Practical Model Fitting Approaches to the Direct Extraction of NMR Parameters Simultaneously from All Dimensions of Multidimensional NMR Spectra,” J. Biomol. NMR 12, 277297 (1998).

263. A. M. Prantner, B. F. Volkman, S. J. Wilkens, B. Xia, and J. L. Markley, “Assignment of 1H, 13C, and 15N Signals of Reduced Clostridium pasteurianum Rubredoxin: Oxidation StateDependent Changes in Chemical Shifts and Relaxation Rates,” J. Biomol. NMR 10, 411412 (1997).

264. K. E. Prehoda, E. S. Mooberry, and J. L. Markley, “High Pressure Effects on Protein Structure,” In Protein Dynamics, Function and Design (O. Jardetzky and J.F. Lefvre, Eds.), NATO ASI Series, Plenum Press, pp. 5986 (1998).

265. B. Xia, B. F. Volkman, and J. L. Markley, “Evidence for OxidationStateDependent Conformational Changes in Human Ferredoxin from Multinuclear, Multidimensional NMR Spectroscopy,” Biochemistry 37, 39653973 (1998).

266. J. E. Caldwell, F. Abildgaard, D. Ming, G. Hellekant, and J. L. Markley, “Complete 1H and Partial 13C Resonance Assignments at 37 and 22 C for Brazzein, an Intensely Sweet Protein,” J. Biomol. NMR 11, 231232 (1998).

267. S. Choe, Ž. Džakula, E. S. Kulog˘lu, and J. L. Markley, “Assignment of 1H, 13C, and 15N Signals of Turkey Ovomucoid Third Domain at pH 2.0,” J. Biomol. NMR 12, 193195 (1998).

268. M. Hirasawa, J. K. Hurley, Z. Salamon, G. Tollin, J. L. Markley, H. Cheng, B. Xia, and D. B. Knaff, “The Role of Aromatic and Acidic Amino Acids in the Electron Transfer Reaction Catalyzed by Spinach FerredoxinDependent Glutamate Synthase,” Biochim. Biophys. Acta 1363, 134146 (1998).

269. S. J. Wilkens, B. Xia, B. F. Volkman, F. Weinhold, J. L. Markley, and W. M. Westler, “Inadequacies of the PointDipole Approximation for Describing ElectronNuclear Interactions in Paramagnetic Proteins: Hybrid Density Functional Calculations and the Analysis of NMR Relaxation of HighSpin Iron(III) Rubredoxin,” J. Phys. Chem. B. 102, 83008305 (1998).

270. B. Xia, S. J. Wilkens, W. M. Westler, and J. L. Markley, “Amplification of OneBond 1H/2H Isotope Effects on 15N Chemical Shifts in Clostridium pasteurianum Rubredoxin by FermiContact Effects through Hydrogen Bonds,” J. Am. Chem. Soc. 120, 48934894 (1998).

271. J. E. Caldwell, F. Abildgaard, Ž. Džakula, D. Ming, G. Hellekant, and J. L. Markley, “Solution Structure of the Thermostable SweetTasting Protein Brazzein,” Nature Structural Biology 5, 427431 (1998).

272. Ž. Džakula, N. Juranić, M. L. DeRider, W. M. Westler, S. Macura, and J. L. Markley, “Analysis of Error Propagation from NMRDerived Internuclear Distances into Molecular Structure of CycloProGly,” J. Magn. Reson. 135, 454465 (1998).

273. K. E. Prehoda, E. S. Mooberry, and J. L. Markley, “Pressure Denaturation of Proteins: Evaluation of Compressibility Effects,” Biochemistry 37, 57855790 (1998).

274. M. E. Girvin, V. K. Rastogi, F. Abildgaard, J. L. Markley, and R. H. Fillingame, “Solution Structure of the Transmembrane H+Translocating Subunit c of the F1F0 ATP Synthase,” Biochemistry 37, 88178824 (1998).

275. B. F. Volkman, S. L. Alam, J. D. Satterlee, and J. L. Markley, “Solution Structure and Backbone Dynamics of Component IV Glycera dibranchiata Monomeric HemoglobinCO,” Biochemistry 37, 1090610919 (1998).

276. G. Kaslik, W. M. Westler, L. Gráf, and J. L. Markley, “Properties of the His57Asp102 Dyad of Rat Trypsin D189S in the Zymogen, Activated Enzyme, and 1Proteinase Inhibitor Complexed Forms,” Arch. Biochem. Biophys. 362, 254264 (1999).

277. Y. K. Chae, F. Abildgaard, E. R. Chapman, and J. L. Markley, “Lipid Binding Ridge on Loops 2 and 3 of the C2A Domain of Synaptotagmin I as Revealed by NMR Spectroscopy,” J. Biol. Chem. 273, 2565925663 (1998).

278. L. Wang, Y. Li, F. Abildgaard, J. L. Markley, and H. Yan, “NMR Solution Structure of Type II Human Cellular Retinoic Acid Binding Protein: Implications for Ligand Binding,” Biochemistry 37, 1272712736 (1998).

279. B. Xia, J. D. Pikus, W. Xia, K. McClay, R. J. Steffan, Y. K. Chae, W. M. Westler, J. L. Markley, and B. G. Fox, “Detection and Classification of HyperfineShifted 1H, 2H, and 15N Resonances of the Rieske Ferredoxin Component of Toluene 4Monooxygenase,” Biochemistry 38, 727739 (1999).
GM35976, NIH RR02301

280. J. Schleucher, P. Vanderveer, J. L. Markley, and T. D. Sharkey, “Disequilibrium of Chloroplastic Phosphoglucose Isomerase Inferred from Deuterium Isotope Discrimination,” In Photosynthesis: Mechanisms and Effects (G. Garab, Ed.), Kluwer Academic Publishers, Vol. V, pp. 35213524 (1998).

281. J. Lin, W. M. Westler, W. W. Cleland, J. L. Markley, and P. A. Frey, “Fractionation Factors and Activation Energies for Exchange of the Low Barrier Hydrogen Bonding Proton in Peptidyl Trifluoromethyl Ketone Complexes of Chymotrypsin,” Proc. Natl. Acad. Sci. USA, 95, 1466414668 (1998).

282. B. F. Volkman, M. E. Anderson, K. D. Clark, Y. Hoyakawa, M. R. Strand, and J. L. Markley, “Structure of the Insect Cytokine Peptide PlasmatocyteSpreading Peptide 1 from Pseudoplusia includens,” J. Biol. Chem. 274, 44934496 (1999).

283. J. Schleucher, P. Vanderveer, J. L. Markley, and T. D. Sharkey, “Intramolecular Deuterium Distributions Reveal Disequilibrium of Chloroplastic Phosphoglucose Isomerase,” Plant, Cell and Environment 22, 525533 (1999).

284. B. F. Volkman, S. J. Wilkens, A. L. Lee, B. Xia, W. M. Westler, R. Beger, and J. L. Markley, “RedoxDependent Magnetic Alignment of Clostridium pasteurianum Rubredoxin: Measurement of Magnetic Susceptibility Anisotropy and Prediction of Pseudocontact Shift Contributions,” J. Am. Chem. Soc. 121, 46774683 (1999).

285. M. A. Qasim, S. M. Lu, J. Ding, K. S. Bateman, M. N. G. James, S. Anderson, J. Song, J. L. Markley, P. J. Ganz, C. W. Saunders, and M. Laskowski, Jr., “Thermodynamic Criterion for the Conformation of P1 Residues of Substrates and of Inhibitors in Complexes with Serine Proteinases,” Biochemistry 38, 71427150 (1999).

286. R. W. Curley, Jr., A. K. Sundaram, J. W. Fowble, F. Abildgaard, W. M. Westler, and J. L. Markley, “NMR Studies of RetinoidProtein Interactions: The Conformation of [13C]Ionones Bound to Lactoglobin B,” Pharmaceutical Research, 16, 651659 (1999).

287. Y. K. Chae, F. Abildgaard, C. A. Royer, and J. L. Markley, “Oligomerization of the EK18 Mutant of the trp Repressor of Escherichia coli as Observed by NMR Spectroscopy,” Arch. Biochem. Biophys. 371, 3540 (1999).

288. B. Xia, D. Jenk, D. M. LeMaster, W. M. Westler, and J. L. Markley, “ElectronNuclear Interactions in Two Prototypical [2Fe2S] Proteins: Selective (Chiral) Deuteration and Analysis of 1H and 2H NMR Signals from the Alpha and Beta Hydrogens of Cysteinyl Residues that Ligate the Iron in the Active Sites of Human Ferredoxin and Anabaena 7120 Vegetative Ferredoxin,” Arch. Biochem. Biophys. 373, 328334 (2000).

289. F. M. AssadiPorter, D. J. Aceti, H. Cheng, and J. L. Markley, “Efficient Production of Recombinant Brazzein, a Small, HeatStable, SweetTasting Protein of Plant Origin,” Arch. Biochem. Biophys. 376, 252258 (2000).

290. F. M. AssadiPorter, D. J. Aceti, and J. L. Markley, “Sweetness Determinant Sites of Brazzein, a Small, HeatStable, SweetTasting Protein,” Arch. Biochem. Biophys. 376, 259265 (2000).

291. H. Hemmi, J. M. Studts, Y. K. Chae, J. L. Markley, and B. G. Fox, “Assignment of 1H, 13C, and 15N NMR Signals in the Toluene 4Monooxygenase Effector Protein,” J. Biomol. NMR, 16, 359360 (2000).

292. Y. K. Chae and J. L. Markley, “Functional Recombinant Rabbit Muscle Phosphoglucomutase from Escherichia coli,” Protein Expr. Purif., 20 124127 (2000).

293. H. Hemmi, J. M. Studts, Y. K. Chae, J. Song, J. L. Markley, and B. G. Fox, “Solution Structure of the Toluene4 Monooxygenase Effector Protein (T4moD),” Biochemistry, 40, 3512-3524 (2001).

294. J. Song, and J. L. Markley, “NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the 1H, 13C and 15N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin A,” J. Mol. Recognition. 14, 166-171 (2001).

295. D. Chen, A. L. Zangl, Q Zhao, J. L. Markley, J. Zheng, I. M. Bird, R. R. Magness, “Ovine caveolin-1: cDNA cloning E. coli expression, and association with endothelial nitric oxide synthase,” Mol. Cell. Endrochrinol. 175, 41-56 (2001).

296. S. J. Wilkens, W. M. Westler, J. L. Markley, and F. Weinhold, “Natural J-Coupling Analysis: Interpretation of Scalar J-Couplings in Terms of Natural Bond Orbitals” J. Am. Chem. Soc. 123, 12026-12036 (2001).

297. E. S. Kulog˘lu, D. R. McCaslin, M. Kitabwalla, C. D. Pauza, J. L., Markley, and B. F. Volkman, “Monomeric Solution Structure for the Prototypical ‘C’ Chemokine Lymphotactin,” Biochemistry, 40, 12486-12496 (2001).

298. W. Luo, L. A. Moe, L. Skjeldal, J. D. Pikus, F. Abildgaard, J. L. Markley, and B. G. Fox, “Assignment of 1H, 13C and 15N NMR signals from toluene 4-monooxygenase Rieske ferredoxin in its oxidized state” J. Biomol. NMR 21, 73-74 (2001).

299. W. F. Walkenhorst, J. A. Edwards, J. L. Markley, and H. Roder, “Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange,” Protein Science, 11, 82-91 (2002).

300. M. L. DeRider, S. J. Wilkens, M. J. Waddell, L. E. Bretscher, F. Weinhold, R. T. Raines, and J. L. Markley, “Collagen Stability: Insights from NMR Spectroscopic and Hybrid Density Functional Computational Investigations of the Effect of Electronegative Substituents on Prolyl Ring Conformation,” J. Am. Chem. Soc., 124, 2497-2505 (2002).

301. T. E. Machonkin, W. M. Westler, and J. L. Markley, “13C{13C} 2D NMR: a Novel Strategy for the Study of Paramagnetic Proteins with Slow Electronic Relaxation Rates,” J. Am. Chem. Soc. 124, 3204-3205 (2002).

302. J. L. Markley, E. L. Ulrich, W. M. Westler, and B. F. Volkman, “Macromolecular Structure Determination by NMR,” In Structural Bioinformatics (H. Weissig, and P. Bourne,eds.), Wiley and Sons, New York, 2003.

303. T. E. Machonkin and J. L. Markley, Electron-Nuclear Interactions in Iron-Sulfur Proteins, In Encyclopedia of Nuclear Magnetic Resonance: Supplementary Volume, (D. M. Grant and R. K. Harris, eds), John Wiley & Sons, Ltd, New York, pp. 384-401, 2002.

304. S. J. Wilkens, W. Westler, F. Weinhold, and J. L. Markley, “Trans-Hydrogen-Bond h2JNN and h1JNH Couplings in the DNA A–T Base Pair: Natural Bond Orbital Analysis,” J. Am. Chem. Soc. 124, 1190-1191 (2002).

305. W. M. Westler, P. A. Frey, J. Lin, D. Wemmer, P. G. Williams, and J. L. Markley, “Evidence for a Strong Hydrogen Bond in the Catalytic Dyad of Transition State Analog Inhibitor Complexes of Chymotrypsin from Proton–Triton NMR Chemical Shift Differences,” J. Am. Chem. Soc. 124, 4196-4197 (2002).

306. O. Y. Dmitriev, F. Abildgaard, J. L. Markley, and R. H. Fillingame, “Structure of Ala24/Asp61→Asp24/Asn61 Substituted Subunit c of Escherichia coli ATP Synthase: Implications for the Mechanism of Proton Transport and Rotary Movement in the Fo Complex,” Biochemistry 41, 5537-5547 (2002).

307. E. S. Kulog˘lu, D. R. McCaslin, J. L. Markley, and B. F. Volkman, “Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions,” J. Biol. Chem. 277, 17863-17870 (2002).

308. R. Fogh, J. Ionides, E. Ulrich, W. Boucher, W. Vranken, J. P. Linge, M. Habeck, W. Rieping, T. N. Bhat, J. Westbrook, K. Henrick, G. Gilliland, H. Berman, J. Thornton, M. Nilges, J. L. Markley, and E. Laue, “The CCPN project: an interim report on a data model for the NMR community,” Nature Struct. Biol. 9, 416-418 (2002).

309. B. J. Goodfellow, S. G. Nunes, F. Rusnak, I. Moura, C. Ascenso, J. J. G. Moura, B. F. Volkman, and J. L. Markley, “Pseudocontact shifts in Desulfovibrio gigas desulforedoxin”, Protein Sci. 11, 2464-2470 (2002).

310. Q. Zhao, Y. K. Chae, and J. L. Markley “NMR Solution Structure of ATTp an Arabidopsis thaliana Trypsin Inhibitor,” Biochemistry 41, 12284-12296 (2002).

311. M. A. Kennedy, G. T. Montelione, C. H. Arrowsmith, and J. L. Markley, “A Role for NMR in Structural Genomics,” Journal of Structural and Functional Genomics 2, 155-169 (2002).

312. Z. Zolnai, P. T. Lee, J. Li, M. R. Chapman, C. S. Newman, G. N. Phillips, Jr., I. Rayment, E. L. Ulrich, B. F. Volkman, and J. L. Markley, “Project Management System for Structural and Functional Proteomics: Sesame,” J. Structural and Functional Genomics 4, 11–23 (2003).

313. W. M Westler, F. Weinhold, and J. L. Markley, “Quantum Chemical Calculations on Structural Models of the Catalytic Site of Chymotrypsin: Comparison of Calculated Results with Experimental Data from NMR Spectroscopy,” J. Am. Chem. Soc. 124, 14373-14381 (2002).

314. F. A. J. Rotsaert, J. D. Pikus, B. G. Fox, J. L. Markley, J. Sanders-Loehr, “N-Isotope effects on the Raman Spectra of Fe2S2 Ferredoxins and Rieske Ferredoxins: Evidence for Structural Rigidity of Metal Sites,” J. Biol. Inorg. Chem. 8, 318-326 (2003).

315. J. Song, M. Laskowski, Jr., M. A. Qasim, and J. L Markley, “NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme – Inhibitor Contact Position of Turkey Ovomucoid Third Domain,” Biochemistry 42, 2847-2856 (2003).

316. I-J. Lin, E. B. Gebel, T. E. Machonkin, W. M. Westler, and J. L. Markley, "Correlation between Hydrogen Bond Lengths and Reduction Potentials in Clostridium pasteurianum Rubredoxin," J. Am. Chem. Soc. 125, 1464-1465 (2003).

317. J. F. Doreleijers, S. Mading, D. Maziuk, K. Sojourner, L. Yin, J. Zhu, J. L. Markley, and E. L. Ulrich, “BioMagResBank database with sets of experimental NMR constraints corresponding to the structures of over 1400 biomolecules deposited in the Protein Data Bank,” J. Biomolecular NMR 26, 139-146 (2003).

318. J. Song and J. L. Markley, “Protein Inhibitors of Serine Proteinases: Role of Backbone Structure and Dynamics in Controlling the Hydrolysis Constant,” Biochemistry 42, 5186-5194 (2003).

319. J. Song, M. Laskowski, Jr., M. A. Qasim, and J. L Markley, “Two Conformational States of Turkey Ovomucoid Populated at Low pH: Three-Dimensional Structures, Internal Dynamics, and Interconversion Kinetics and Thermodynamics,” Biochemistry 42, 6380-6391 (2003).

320. F. M. Assadi-Porter, F. Abildgaard, H. Blad, and J. L. Markley, “Correlation of the Sweetness of Variants of the Protein Brazzein with Patterns of Hydrogen Bonds Detected by NMR Spectroscopy,” J. Biol. Chem. 278, 32331-31339 (2003).

321. Z. Jin, V. Danilova, F. M. Assadi-Porter, D. J. Aceti, J. L. Markley, and G. Hellekant, “Critical Regions for the Sweetness of Brazzein,” FEBS Lett. 544, 33-37 (2003).

322. W-.J. Wu, G. Vidugiris, E. S. Mooberry, W. M. Westler, J. L. Markley, “Mixing Apparatus for Preparing NMR Samples under Pressure,” J. Magn. Reson. 164, 84-91 (2003).

323. J. L. Markley, E. L. Ulrich, W. M. Westler, and B. F. Volkman, “Macromolecular Structure Determination by NMR Spectroscopy,” Methods Biochem. Anal. 44, 89-113 (2003).

324. Z. Jin, V. Danilova, F. M. Assadi-Porter, J. L. Markley, and G. Hellekant, “Monkey Electrophysiological and Human Psychophysical Responses to Mutants of the Sweet Protein Brazzein: Delineating Brazzein Sweetness,” Chemical Senses 28, 491-498 (2003).

325. Q. Zhao, R. Frederick, K. Seder, S. Thao, H. Sreenath, F. Peterson, B. F. Volkman, J. L. Markley, and B. G. Fox, “Production in Two-Liter Beverage Bottles of Proteins for NMR Structure Determination Labeled with Either 15N- or 13C-15N,” J. Struct. Funct. Genomics, 5, 87-93 (2004).

326. Y. K. Chae, H. Im, Q. Zhao, J. H. Doelling, R. D. Vierstra, and J. L. Markley, “Prevention of Aggregation after Refolding by Balanced Stabilization-Destabilization: Production of the Arabidopsis thaliana Protein At4g21980 (APG8a) for NMR Structure Determination” Protein Prod. Purif. 34, 280-283 (2004).

327. G. Cornilescu, C. C. Cornilescu, Q. Zhao, R. O. Frederick, F. C. Peterson, S. Thao, and J. L. Markley, “Solution Structure of a Homodimeric Hypothetical Protein, At5g22580, a Structural Genomics Target from Arabidopsis thaliana,” J. Biomol. NMR 29, 387-390 (2004).

328. T. E. Machonkin, W. M. Westler, and J. L. Markley, “Novel Strategy for the Study of Paramagnetic Proteins with Slow Electronic Relaxation Rates by NMR Spectroscopy: Application to Oxidized Human [2Fe-2S] Ferredoxin,” J. Amer. Chem. Soc. 126, 5413-5426 (2004).

329. O. Yu. Dmitriev, F. Abildgaard, J. L. Markley, and R. H. Fillingame, “Backbone 1H, 15N and 13C Assignments for the Subunit a of the E. coli ATP Synthase,” J. Biomol. NMR 29, 439-440 (2004).

330. C. A. Bingman, K. A. Johnson, F. C. Peterson, R. O. Frederick, Q. Zhao, S. Thao, B. G. Fox, B. F. Volkman, W. B. Jeon, D. W. Smith, C. S. Newman, E. L. Ulrich, A. Hegeman, M. R. Sussman, J. L. Markley, and G. N. Phillips, Jr., “Crystal structure of the protein from gene At3g17210 of Arabidopsis thaliana, Proteins 57, 218-220 (2004).

331. I. Y. Park, M. K. Eidsness, I-J. Lin, E. B. Gebel, .B. Youn, J. L. Harley, T. E. Machonkin, R. O. Frederick, J. L. Markley, E. Smith, T. Ichiye, and C.H. Kang, “Crystallographic studies of V44 mutants of Clostridium pasteurianum rubredoxin: Effects of side chain size on reduction potential,” Proteins 57, 618-625 (2004).

332. J. Song, D. A. Vinarov, E. M. Tyler, M. N. Shahan, R. C. Tyler, and J. L. Markley, “Hypothetical protein At2g24940.1 from Arabidopsis thaliana has a cytochrome b5 like fold,” J. Biomol. NMR 30, 215-218 (2004).

333. L. Skjeldal, F. C. Peterson, L. A. Moe, J. D. Pikus, J. F. Doreleijers, B. F. Volkman, W. M. Westler, J. Markley and B. G. Fox, “Solution Structure of T4moC, the Rieske Ferredoxin Component of the Toluene 4-Monooxygenase Complex,” J. Inorg. Biol. Chem. 9, 945-953 (2004).

334. D. W. Smith, K. A. Johnson, C. A. Bingman, D. J. Aceti, P. G. Blommel, R. L. Wrobel, R. O. Frederick, Q. Zhao, H. Sreenath, B. G. Fox, B. F. Volkman, W. B. Jeon, C. S. Newman, E. L. Ulrich, A. D. Hegeman, T. Kimball, S. Thao, M. R. Sussman, J. L. Markley, and George N. Phillips Jr., “Crystal Structure of At2g03760, a Putative Steroid Sulfotransferase from Arabidopsis thaliana,” Proteins 57, 854-857 (2004).

335. D. A. Vinarov, B. L. Lytle, F. C. Peterson, E. M. Tyler, B. F. Volkman, and J. L. Markley, “Cell-free protein production and labeling protocol for NMR-based structural proteomics,” Nature Methods 1, 149-153 (2004).

336. F. M. Assadi-Porter, F. Abildgaard, H. Blad, C. C. Cornilescu, and J. L. Markley, “Brazzein, a small sweet protein: effects of mutations on its structure, dynamics, and functional properties, Chemical Senses 30 Suppl. 1: i90-i91 (2005).

337. J. Song, Q. Zhao, S. Thao, R. O. Frederick, and J. L. Markley, “Solution structure of a calmodulin-like calcium-binding domain from Arabidopsis thaliana,” J. Biomol. NMR 30, 451-456 (2004).

338. B. L. Lytle, F. C. Peterson, S.-H. Qiu, M. Luo, Q. Zhao, J. L. Markley, and B F. Volkman, Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B, J. Biol. Chem. 297, 46787-46793 (2004).

339. T. E. Malone, S. E. Madson, R. L. Wrobel, W. B. Jeon, N. S. Rosenberg, K. A. Johnson, C. A. Bingman, D. W. Smith, G. N. Phillips, Jr., J. L. Markley, and B. G. Fox, “X-Ray Structure of Arabidopsis At2g06050, 12-Oxophytodienoate Reductase Isoform 3, Proteins 58, 243-245 (2005).

340. N. Sugimori, T. Torizawa, D. J. Aceti, S. Thao, J.. L. Markley, and M. Kainosho, “1H, 13C and 15N backbone assignment of a 32 kDa hypothetical protein from Arabidopsis thaliana, At3g16450.1,” J. Biomol. NMR 30, 357-358 (2004).

341. A. J. Nederveen, J.F. Doreleijers,W. Vranken, Z. Miller, C. A. E. M. Spronk, S. B. Nabuurs, P. Güntert, M. Livny, J. L. Markley, M. Nilges, E. L. Ulrich, R. Kaptein, and A. M. J. J. Bonvin, “RECOORD: a REcalculated COORdinates Database of 500+ proteins generated from restraint data downloaded from the BioMagResBank,” Proteins 59, 662-272 (2005).

342. C. J. Oldfield, E. L. Ulrich, Y. G. Cheng, A. K. Dunker, and J. L. Markley, “Addressing the Intrinsic Disorder Bottleneck in Structural Proteomics,” Proteins 59, 444-453 (2005).

343. R. C. Tyler, D.J. Aceti, C.A. Bingman, C.C. Cornilescu, B.G. Fox, R.O. Frederick, W.B. Jeon, M.S. Lee, C.S. Newman, F.C. Peterson, G.N. Phillips, Jr., M.N. Shahan, S. Singh, J. Song, H. Sreenath, E. M. Tyler, E.L. Ulrich, D. A. Vinarov, F. C. Vojtek, B. F. Volkman, R.L. Wrobel, Q. Zhao, and J.L. Markley, “Comparison of cell-based and cell-free protocols for producing target proteins from the Arabidopsis thaliana genome for structural studies,” Proteins 59, 633-643 (2005).

344. W. F. Vranken, W. Boucher, T. J. Stevens, R. H. Fogh, A. Pajon, M. Llinas, E. Ulrich, J. Markley, J. Ionides and E. D. Laue, “The CCPN Data Model for NMR Spectroscopy: Development of a Software Pipeline for HTP projects,” Proteins 59, 687-696 (2005).

345. R. C. Tyler, H K. Sreenath, D. J. Aceti, C A. Bingman, S. Singh, J. L. Markley and B. G. Fox, “Auto-Induction Medium for the Production of [U-15N]- and [U-13C, U-15N]-labeled Proteins for NMR Screening and Structure Determination,” Protein Exp. Purif. 40, 268278 (2005).

346. D. A. Vinarov and J. L. Markley, “High-Throughput Automated Platform for NMR-Based Structural Proteomics,” Expert Review of Proteomics 2, 4955 (2005).

347. T. E. Machonkin, W. M. Westler, and J. L. Markley, “Paramagnetic NMR Spectroscopy and Density Functional Calculations in the Analysis of the Geometric and Electronic Structures of Iron-Sulfur Proteins,” Inorg. Chem. 44, 779797 (2005).

348. J. F. Doreleijers, A. J. Nederveen, W. Vranken, J. Lin, A. M. J. J. Bonvin, R. Kaptein, J. L. Markley, and E. L. Ulrich, “BioMagResBank databases DOCR and FRED with converted and filtered sets of experimental NMR restraints and coordinates from over 500 protein PDB structures,” J. Biomol. NMR 32, 112 (2005).

349. J. Song, R. C. Tyler, R. L. Wrobel, R. O. Frederick, F. C. Vojtek, W. B. Jeon, M. S. Lee, J. L. Markley, “Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein, Protein Sci. 14, 10591063 (2005).

350. L. Wang, H. R. Eghbalnia, A. Bahrami, and J. L. Markley, Linear analysis of carbon-13 chemical shift differences and its application to the detection and correction of errors in referencing and spin system identifications,” J. Biomol. NMR 32, 1322 (2005).

351. V. Stolc, M. P. Samanta, W. Tongprasit, H. Sethi, S. Liang, D. C. Nelson A. Hegeman, C Nelson, D. Rancour, S. Bednarek, E. L. Ulrich, Q. Zhao, R. L. Wrobel, C. S. Newman, B. G. Fox, G. N. Phillips, Jr., J. L. Markley, and M. R. Sussman, “Identification of Novel Transcribed Sequences in Arabidopsis thaliana using High-Resolution Genome Tiling Arrays,” Proc. Natl. Acad. Sci. USA 102, 44534458 (2005).

352. H. R. Eghbalnia, L. Wang, A. Bahrami, A. Assadi, and J. L. Markley, “Protein Energetic Conformational Analysis from NMR Chemical Shifts (PECAN) and its use in Determining Secondary Structural Elements,” J. Biomol. NMR 32, 7181 (2005).

353. E. Bitto, C. A. Bingman, S. T. M. Allard, G. E. Wesenberg, D. J. Aceti, R. L. Wrobel, R. O. Frederick, H. Sreenath, F. C. Vojtik, W. B. Jeon, C. S. Newman, J. Primm, M. R. Sussman, B. G. Fox, J. L. Markley, and G. N. Phillips Jr., “The structure at 2.4 Å resolution of the protein from gene locus At3g21360, a putative FeII/2-oxoglutarate-dependent enzyme from Arabidopsis thaliana,” Acta Cryst. F61, 469–472 (2005).

354. H. R. Eghbalnia, A. Bahrami, L. Wang, A. Assadi, and J. L. Markley, “Probabilistic Identification of Spin Systems and their Assignments including Coil-Helix Inference as Output (PISTACHIO),” J. Biomol. NMR 32, 219233 (2005).

355. F. C. Peterson, B. L. Lytle, S. Sampath, D. Vinarov, E. Tyler, M. Shahan, J. L. Markley, and B. F. Volkman, “Solution Structure of Thioredoxin h1 from Arabidopsis thaliana,” Protein Sci. 14, 2195-2200 (2005).

356. J. Song, Q, Zhao, M. S. Lee, and J. L. Markley, “1H, 15N and 13C resonance assignments of the putative Bet v 1 family protein At1g24000.1 from Arabidopsis thaliana,” J. Biomol. NMR 32, 335 (2005).

357. Y. K. Chae, K. Lee, and J. L. Markley, “1H, 15N and 13C resonance assignments of a protein involved in the autophagy process, At4g21980.1 from Arabidopsis thaliana,” J. Biomol. NMR 32, 337 (2005).

358. S. Singh, C. C. Cornilescu, R. C. Tyler, G. Cornilescu, M. Tonelli, M. S. Lee, and J. L. Markley, “Solution Structure of a Late Embryogenesis Abundant (LEA14) Protein from Arabidopsis thaliana, a Cellular Stress Related Protein,” Protein Sci. 14, 2601-2609 (2005).

359. Q. Zhao, J. Song, Z. Jin, V. Danilova, G. Hellekant, and J.L. Markley, “Probing the sweet determinants of brazzein: Wild-type brazzein and a tasteless variant, brazzein-ins(R18a-I18b), exhibit different pH-dependent NMR chemical shifts,” Biochem. Biophys. Res. Commun. 335, 256-263 (2005).

360. K. Uchida, J. L. Markley, and M. Kainosho, “Carbon-13 NMR method for the detection of correlated hydrogen exchange at adjacent backbone peptide amides and its application to hydrogen exchange in five anti-parallel -strands within the hydrophobic core of Streptomyces subtilisin inhibitor (SSI), Biochemistry 44, 1181111820 (2005).

361. H. R. Eghbalnia, A. Bahrami, M. Tonelli, K. Hallenga, and J. L. Markley, “High Resolution Iterative Frequency Identification for NMR (HIFI-NMR) as a General Strategy for Multidimensional Data Collection,” J. Am. Chem. Soc 127, 12528-12536 (2005). PMCID in process #6770.

362. S. Singh, M. Tonelli, R. C. Tyler, A Bahrami, M. S. Lee, and J. L. Markley, “Three-dimensional structure of the AAH26994.1 protein from Mus musculus, a putative eukaryotic Urm1,” Protein Sci. 14, 2095-2102 (2005).

363. H. Blad, N. J. Reiter, F. Abildgaard, J. L. Markley, and S. E. Butcher, “Dynamics and metal ion binding in the U6 RNA intramolecular stem-loop as analyzed by NMR,” J. Mol. Biol. 353, 540-555 (2005).

364. I-J. Lin, E. B. Gebel, T. E. Machonkin, W. M. Westler, J. L. Markley, “Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants,” Proc. Natl. Acad. Sci. USA 102, 14581-14586 (2005).

364a. B. G. Fox, T. E. Malone, K. A. Johnson, S. E. Madson, D. Aceti, C. A. Bingman, B. G. Blommel, B. Buchan, B. Burns, J. Cao, C. Cornilescu, J. Doreleijers, J. Ellefson, R. Frederick, A Geetha, D. Hruby, W. B. Jeon, T. Kimball, J. Kunert, J. L. Markley, C. Newman, A. Olson, F. C. Peterson, G. N. Phillips, Jr., J. Primm, B. Ramirez, N. S. Rosenberg, M. Runnels, K. Seder, J. Shaw, D. W. Smith, D. H. Sreenath, J. Song, M. R. Sussman, S. Thao, D. Troestler, E. Tyler, R. Tyler, E. Ulrich, D. Vinarov, F. Vojtik, B. F. Volkman, G. Wesenberg, R. L. Wrobel, J. Zhang, Q. Zhao, and Z. Zolani, “X-ray structure of Arabidopsis Atlg77680, 12-oxophytodienoate reductase isoform 1,” Proteins 61, 206-208 (2005).

365. Q. Cui, M. P. Thorgersen, W. M. Westler, J. L. Markley, and D. M. Downs, “Solution structure of YggX: a prokaryotic protein involved in Fe(II) trafficking,” Proteins 62, 578-586 (2006).

366. J. Song, R. C. Tyler, M. S. Lee, E. M. Tyler, and J. L. Markley, “Solution structure of isoform 1 of Roadblock/LC7, a light chain in the dynein complex,” J. Mol. Biol. 354, 10431051 (2005).

367. R. K. Andjus, Z. Dzakula, J. L. Markley, and S. Macura, “Brain Energetics and Tolerance to Anoxia in Deep Hypothermia,” Ann. N.Y. Acad. Sci. 1048, 1035 (2005).

368. D. A. Vinarov, C. L. Newman, E. M. Tyler, J. L. Markley, M. N. Shahan, “Wheat germ cell-free expression system for protein production,” Curr. Protoc. Protein Sci. Chapter 5:Unit 5.18. (2006). PMID: 18429309.

369. G. A. Zornetzer, R. D. White, J. L. Markley, and B. G. Fox, “Preparation of Isotopically Labeled Spinach Acyl-Acyl Carrier Protein for NMR Structural Studies,” Protein Exp. Purif. 46, 446455 (2006).

370. J. L. Markley, “Protein Solution Structure in Three Days or Less?,” The Scientist 19, 3640 (2005).

371. H.-C. Ahn, N. Juranic, S. Macura, and J. L. Markley, “Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent-exposed surface,” J. Am. Chem. Soc. 128, 4398-4404 (2006).

372. O. Dmitriev, R. Tsivkovskii, F. Abildgaard, C. T. Morgan, J. L. Markley, and S. Lutsenko, “Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutations,” Proc. Natl. Acad. Sci. USA 103, 53025307 (2006).

374. L. Wang, H. R. Eghbalnia, and J. L. Markley, “Probabilistic approach to determining unbiased random-coil carbon-13 chemical shift values from the protein chemical shift database,” J. Biomol. NMR 35, 155165 (2006).

375. B. L. Lytle, F. C. Peterson, E. M. Tyler, D. A. Vinarov, J. L. Markley and B. F. Volkman, “Solution structure of Arabidopsis thaliana protein At5g39720.1, a member of the AIG2-like protein family,” Acta. Cryst. F62, 490493 (2006).

376. L. Guo, F. M. Assadi-Porter, J. E. Grant, H. Wu, J. L. Markley, and A. E. Ruoho, “One-Step Purification of Bacterially Expressed Recombinant Transducin -Subunit and Isotopically Labeled PDE6 -subunit for NMR Analysis, Protein Exp. Purif. 51, 187197 (2007).

377. I-J. Lin, Y. Chen, J. A. Fee, J. Song, W. M. Westler, and J. L. Markley, “Rieske Protein from Thermus thermophilus: 15N NMR Titration Study Demonstrates the Role of Iron-Ligated Histidines in the pH Dependence of the Reduction Potential,” J. Am. Chem. Soc. 128, 1067210673 (2006).

378. D. A. Vinarov, C L. Loushin Newman, and J. L. Markley, “Wheat Germ Cell-Free Platform for Eukaryotic Protein Production,” invited Mini Review, FEBS J. 273, 41604169 (2006).

379. S. Singh, M. H. Hager, C. Zhang, B. R. Griffith, M. S. Lee, K. Hallenga, J. L. Markley, and J. S. Thorson, “Structural insight into self-sacrifice mechanism of enediyne resistance,” ACS Chem. Biol. 1, 451460 (2006).

380. J. L. Markley, “NMR-Based Structural Proteomics,” In, Spectral Techniques in Proteomics, D. S. Sem, Ed., pp. 350-367, CRC Press, Taylor & Francis Group, Boca Raton, FL (2007).

381. H. M. Berman, S. K. Burley, W. Chiu, A. Sali, A. Adzhubei, P. E. Bourne, S. H. Bryant, R L. Dunbrack, Jr., K. Fidelis, J. Frank, A. Godzik, K. Henrick, A. Joachimiak, B. Heymann, D. Jones, J. L. Markley, J. Moult, G. T. Montelione, C. Orengo, M. G. Rossmann, B. Rost, H. Saibil, T. Schwede, D. M. Standley, and J. D. Westbrook, “Outcome of a workshop on archiving structural models of biological macromolecules.,” Structure 14, 1211–1217 (2006).

382. R. L. Wrobel, C. A. Bingman, W. B. Jeon, J. Song, D. A. Vinarov, R. O. Frederick, D. J. Aceti, H. K. Sreenath, Z. Zolnai, F. C. Vojtik, E. Bitto, B. G. Fox, G. N. Phillips, Jr., and J. L. Markley, “Structural Proteomics,” In Plant Proteomics, Ed. Finnie C. (Blackwell Publishing, Oxford) pp 99128 (2006).

383. J. L. Markley, M. E. Anderson, Q. Cui, H. R. Eghbalnia, I. A. Lewis, A. D. Hegeman, J. Li, C. R. Schulte, M. R. Sussman, W. M. Westler, E. L. Ulrich, Z. Zolnai, “New Bioinformatics Resources for Metabolomics,” Pac. Symp. Biocomput. 12, 157168 (2007).

384. R. C. Tyler, E. Bitto, C. E. Berndsen, C. A. Bingman, S. Singh, M. S. Lee, G. E. Wesenberg, J. M. Denu, G. N. Phillips Jr., J. L. Markley, “Structure of Arabidopsis thaliana At1g77540 protein, a minimal acetyltransferase from the COG2388 family,” Biochemistry 45, 1432514336 (2006).

385. G. Cornilescu, E. B. Hadley, M, G. Woll, J. L. Markley, S. H. Gellman, and C.C. Cornilescu, “Solution structure of a small protein containing a fluorinated side chain in the core,” Protein Sci. 16, 1419 (2007). Erratum: Protein Sci 16, 2089 (2007).

386. G. Cornilescu, D. A. Vinarov, E. M. Tyler, J. L. Markley, and C. C. Cornilescu, Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana, Protein Sci. 15, 28362841 (2006).

387. H. Berman, K. Henrick, H. Nakamura, and J. L. Markley, “The Worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data,” Nucleic Acids Res. 35, D301303 (2007).

388. J. Song, M. S. Lee, I. Carlberg, A. V. Vener, J. L Markley, Micelle-induced Folding of Spinach Thylakoid Soluble Phosphoprotein of 9 kDa and its Functional Implications, Biochemistry 45, 1563315643 (2006).

389. J. Song and J. L. Markley, “Three-dimensional structure determined for a subunit of human tRNA splicing endonuclease (Sen15) reveals a novel dimeric fold.,” J. Mol. Biol. 366, 155164 (2007).

390. F. M. Assadi-Porter, M. Tonelli, J. T. Radek, C. C. Cornilescu, and J. L. Markley, “How Sweet it Is: Detailed Molecular and Functional Studies of Brazzein, a Sweet Protein and its Analogs,” In, Sweetness and Sweeteners, Biology, Chemistry and Psychophysics (ACS Symposium Series 979), D. K. Weerasinghe and G. E. DuBois, Eds., American Chemical Society, Washington DC, Ch. 36, pp. 560-572 (2008).

391. H. C. Ahn, Y. T. Le, P. S. Nagchowdhuri, E. F. Derose, C. Putnam-Evans C, R. E. London, J. L. Markley, and K. H. Lim, “NMR characterizations of an amyloidogenic conformational ensemble of the PI3K SH3 domain,” Protein Sci. 15, 25522557 (2006).

392. J. Song and J. L. Markley, “Cautionary Tail: the Presence of an N-terminal Tag on Dynein Light-Chain Roadblock/LC7 Affects its Interaction with a Functional Partner,” Protein & Pept. Lett. 14, 265268 (2007).

393. G. Zornetzer, B. G. Fox,  J. L. Markley, "Solution Structures of Spinach Acyl Carrier Protein with Decanoate and Stearate," Biochemistry 45, 52175227 (2006).

394. S. Haquin, E. Oeuillet, A. Pajon, M. Harris, A.T. Jones, H. van Tilbeurgh, J.L. Markley, Z. Zolnai, and A. Poupon, “Data Management in Structural Genomics: an Overview,” In Methods in Molecular Biology, Vol. 426, Structural Proteomics (B. Kobe, M. Guss, and T. Huber, Eds.) Humana Press, Totowa, New Jersey, pp. 49−79 (2008).

395. J. Song, Q. Zhao, C. Loushin Newman, D. A Vinarov, and J. L. Markley, “Solution structure of human sorting nexin 22,” Protein Sci. 16, 807814 (2007).

396. G. Cornilescu, A. Bahrami, M. Tonelli, J. L. Markley, and H. R. Eghbalnia, “HIFI-C: a robust and fast method for determining NMR couplings from adaptive 3D to 2D projections,” J. Biomol. NMR 38, 341−351 (2007).

397. J. L. Markley, “NMR analysis goes nano.” Nature Biotechnol. 25, 750751 (2007).

398. G. N. Phillips, Jr., B. G. Fox, J. L. Markley, B. F. Volkman, E. Bae, E. Bitto, C. A. Bingman, R. O. Frederick, J. G. McCoy, B. L. Lytle, B. S. Pierce, J. Song, and S. N. Twigger, “Structures of proteins of biomedical interest from the Center for Eukaryotic Structural Genomics, J. Struct. Funct. Genomics 8, 73−84 (2007).

399. M. Tonelli, L. R. Masterson, G. Veglia, and J. L. Markley, “Carbonyl Carbon Label Selective (CCLS) 1H-15N HSQC Experiment for Backbone Assignments of Proteins Incorporating Pairs of 15N- and 13C-Labeled Amino Acids,” J. Biomol. NMR 39, 177−185 (2007).

400. A. D. Hegeman, C. F. Schulte, Qiu Cui, I. A. Lewis, E. L. Huttlin, H. Eghbalnia, A. C. Harms, E. L. Ulrich, J. L. Markley, and M. R. Sussman, “Stable Isotope Assisted Assignment of Elemental Compositions for Metabolomics,” Anal. Chem. 79, 6912−6921 (2007).

401. L. Wang, H. R. Eghbalnia, and J. L. Markley, “Nearest-neighbor Effects on C? and C? Carbon-13 Chemical Shifts in Proteins,” J. Biomol. NMR 39, 247−257 (2007).

402. I. A. Lewis, S. C. Schommer, B. Hodis, K. A. Robb, M. Tonelli, W. M. Westler, M. R. Sussman and J. L. Markley, “Fast and Accurate Method for Determining Molar Concentrations of Metabolites in Complex Solutions from Two-Dimensional 1H-13C NMR Spectra,” Anal. Chem. 79, 9385−9390 (2007).

403. Q. Cui, I. A. Lewis, A. D. Hegeman, M. E. Anderson, J. Li, C. F. Schulte, W. M. Westler, H. R. Eghbalnia, M. R. Sussman, and J. L. Markley, “Madison Metabolomics Consortium Database (MMCD): a practical tool for identifying metabolites from NMR and MS spectral data,” Nature Biotechnology 26, 162−164 (2008).

404. K. Henrick, Z. Feng, W. Bluhm, D. Dimitropoulos, J. F. Doreleijers, S. Dutta, J. L. Flippen-Anderson, J. Ionides, C. Kamada, E. Krissinel, C. Lawson, J. L. Markley, H. Nakamura, R. Newman, Y. Shimizu, J. Swaminathan, S. Valenkar, J. Ory, E. L. Ulrich, W. Vranken, J. Westbrook, R. Yamashita, H. Yang, J. Young, M. Yousufuddin, and H. M. Berman, ”Remediation of the Protein Data Bank Archive,” Nucleic Acids Res. 36, D426−D433 (2008).

405. E. L. Ulrich, H. Akutsu, J. F. Doreleijers, Y. Harano, Y. E. Ioannidis, J. Lin, M. Livny, S. Mading, D. Maziuk, Z. Miller, E. Nakatani, C. F. Schulte, D. E. Tolmie, R. K. Wenger, H. Yao, and J. L. Markley, “BioMagResBank,” Nucleic Acids Res., 36, D402−D408 (2008).

406. R. O. Frederick, L. Bergeman, P. G. Blommel, L. J. Bailey, J. G. McCoy, J. Song, L. Meske, C. A. Bingman, M. Riters, N. A. Dillon, J. Kunert, J. Yoon, A. Lim, M. Cassidy, J. Bunge, D. J. Aceti, J. G. Primm, J. L. Markley, G. N. Phillips, and B. G. Fox, “Small-scale, semi-automated purification of eukaryotic proteins for structure determination,” J. Struct. Funct. Genomics, 8, 153−166 (2007).

407. F. M. Assadi-Porter, S. Patry, and J. L Markley, “Efficient and rapid protein expression and purification of small high disulfide containing sweet protein brazzein in E. coli.” Protein Expr. Purif. 58, 263−268 (2008).

408. X. Pan, G. E. Wesenberg, J. L. Markley, B. G. Fox, G. N. Phillips, Jr., and C. A. Bingman, “A graphical approach to tracking and reporting target status in structural genomics,” J. Struct. Funct. Genomics 8, 209−216. (2007).

409. J. Song, L.-W. Guo, H. Muradov, N. O. Artemyev, A. E. Ruoho, and J. L. Markley, “The intrinsically disordered γ subunit of cGMP phosphodiesterase populates functional secondary and tertiary structures in solution,” Proc. Natl. Acad. Sci. USA 105, 1505−1510 (2008).

410. N. Juranić, J. J. Dannenberg, G. Cornilescu, P. Salvador, E. Atanasova, H.-C. Ahn, S. Macura, J. L. Markley, and F. G. Prendergast, “Structural dependencies of protein backbone 2JNC′ couplings,” Protein Sci. 17, 768−776 (2008).

411. J. L. Markley, E. L. Ulrich, H. M. Berman, K, Henrick, H. Nakamura, and H. Akutsu, “BioMagResBank (BMRB) as a partner in the Worldwide Protein Data Bank (wwPDB): New policies affecting biomolecular NMR depositions,” J. Biomol. NMR 40, 153−155 (2008).

412. C. C. Cornilescu, F. W. Porter, K. Q. Zhao, A. C. Palmenberg, and J. L. Markley, “NMR structure of the mengovirus Leader protein zinc-finger domain,” FEBS Lett. 582, 896−900 (2008).

413. J. L. Markley, A. Bahrami, H. R. Eghbalnia, F. C. Peterson, E. L. Ulrich, W. M. Westler, and B. F. Volkman, “Macromolecular Structure Determination by NMR Spectroscopy,” In Structural Bioinformatics, 2nd Ed., J. Gu, and P. Bourne eds., John Wiley, pp. 93-142 (2009).

414. J. Song, L. Bettendorff, M. Tonelli, J. L. Markley, “Structural Basis for the Catalytic Mechanism of Mammalian 25 kDa Thiamine Triphosphatase,” J. Biol. Chem. 283, 10938-10948 (2008).

415. D. J. Aceti, E. Bitto, A. F. Yakunin, M. Proudfoot, C. A. Bingman, D. W. Smith, R. O. Frederick, H. K. Sreenath, F. C. Vojtik, R. L.Wrobel, B. G. Fox, J. L. Markley, and G N. Phillips, Jr. “Structural and Functional Characterization of a Novel Phosphatase from the Arabidopsis thaliana gene locus At1g05000,” Proteins 73, 241-253 (2008).

416. F. M. Assadi-Porter, M. Tonelli, E. Maillet, K. Hallenga, O. Benard, M. Max, and J. L. Markley, “Direct NMR Detection of the Binding of Functional Ligands to the Human Sweet Receptor, a Heterodimeric Family 3 GPCR,” J. Am. Chem. Soc. 130, 7212−7213 (2008).

417. L. R. Masterson, M. Tonelli, J. L. Markley, and G. Veglia, “Simultaneous Detection and Deconvolution of Congested Spectra Containing Three Isotopically Labeled Species,” J. Am. Chem. Soc. 130, 7818-7819 (2008).

418. A. K. Füzéry, M. Tonelli, D. T. Ta, G. Cornilescu, L. E. Vickery, and J. L. Markley, “Interaction of the co-chaperone HscB with the apo-form of the iron-sulfur scaffold protein IscU as profiled by NMR spectroscopy,” Biochemistry 47, 9394-93404 (2008)

419. G. Cornilescu; A.T. Ulijasz; C. C. Cornilescu; J L Markley; R. D. Vierstra, “Solution Structure of a Cyanobacterial Phytochrome GAF Domain in the Red Light-Absorbing Ground State,” J. Mol. Biol. 383, 403-413 (2008).

420. E. Bitto, C. A. Bingman, L. Bittova, D. A. Kondrashov, R. M. Bannen, B. G. Fox, John L. Markley, and George N. Phillips, Jr., “Structure of Human J-Type Co-chaperone HscB Reveals a Tetracysteine Metal Binding Domain,” J. Biol. Chem. 283, 30184-30192 (2008).

421. J. Song, J. V. McGivern, K. W. Nichols, J. L. Markley, and M. D. Sheets, “Structure and RNA recognition of Xenopus ePABP2: functional implications for Type II poly(A) binding proteins,” Proc. Natl Acad. Sci. USA 105, 15317-15322 (2008).

422. M. Takeda?, N. Sugimori, T. Torizawa, T. Terauchi, A. M. Ono, H. Yagi, Y. Yamaguchi, K. Kato, T. Ikeya, J. G. Jee, P. Güntert, D. J. Aceti??, J. L. Markley??, and M. Kainosho, “Structure of the Putative 32 kDa Myrosinase Binding Protein from Arabidopsis (At3g16450.1) Determined by SAIL-NMR,” FEBS J. 275, 5873-5884 (2008). In process 90680

423. H. M. Berman, K. Henrick, H. Nakamura, and J. L. Markley, “The Worldwide Protein Data Bank,” In Structural Bioinformatics, 2nd Ed., J. Gu, and P. Bourne eds., John Wiley, pp. 293-303 (2009).

424. J. L. Markley, D. J. Aceti, C. A. Bingman, B. G. Fox, R. O. Frederick, S. Makino, K. W. Nichols, G. N. Phillips Jr., J. G. Primm, S. Sahu, F. C. Vojtik, B. F. Volkman, R. L. Wrobel, Z. Zolnai, “The Center for Eukaryotic Structural Genomics.” J. Struct. Funct. Genomics, 2009 Jan 8. [Epub ahead of print].

425. A Bahrami, A. Assadi, J. L. Markley, and H. R. Eghbalnia, “Probabilistic Interaction Network of Evidence Algorithm and its Application to Complete Labeling of Peak Lists from Protein NMR Spectroscopy,” PLoS Comp. Biol. 5(3), e1000307 (2009).

426. G. T. Montelione, C. Arrowsmith, M. E. Girvin, M. A. Kennedy, J. L. Markley, R. Powers, J. H. Prestegard, and T. Szyperski, Unique Opportunities for NMR Methods in Structural Genomics,” J. Struct. Funct. Genomics, 2009 Apr;10(2):101-6. Epub 2009 Mar 15. PMID: 19288278 [PubMed - in process].

427. L. Wang and J. L. Markley, “Empirical Correlation Between Protein Backbone 15N and 13C Secondary Chemical Shifts and its Application to Nitrogen Chemical Shift Re-referencing,” J. Biomol. NMR 44, 95-99 (2009).

428. S-i Makino, M. A. Goren, B. G. Fox, and J. L. Markley, “Cell-free protein synthesis technology in NMR high-throughput structure determination,” in “Cell-free Expression Systems”, Methods in Molecular Biology (K. Takai and Y. Endo, Eds.), The Humana Press Inc., in press.

429. W. Lee, W. M. Westler, A. Bahrami, H. R. Eghbalnia, and J. L. Markley, PINE-SPARKY: graphical interface for evaluating automated probabilistic peak assignments in protein NMR spectroscopy,” Bioinformatics Advance Access, doi: 10.1093/bioinformatics/btp345 (2009). Free access: http://bioinformatics.oxfordjournals.org/cgi/reprint/btp345?ijkey=peLkuo3PlMx58bQ&keytype=ref

430. J. H. Kim, A. K. Füzéry, M. Tonelli, D. T. Ta, W. M. Westler, L. E. Vickery, and J. L. Markley, “Structure and Dynamics of the Iron-Sulfur Cluster Assembly Scaffold Protein IscU and its Interaction with the Cochaperone HscB,” Biochemistry, in press.