Phillips

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Structural Biochemistry

Access the coordinates of structures determined in my lab: via PDB Search

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6607 Biochemistry Addition
Department of Biochemistry
433 Babcock Drive
Madison, WI 53706-1544
USA

Office:
(608) 263-6142
Lab Rooms 6624G, 6606:
(608) 263-5923

   

George N Phillips, Jr.

           

Professor
B.A.: Rice University
Ph.D.: Rice University

      

Structure and dynamics of proteins, computational biology

The overall goal of the research in our laboratory is to relate the three-dimensional structure and dynamics of proteins to their biological functions. We use techniques of X-ray crystallography and electron microscopy to elucidate the molecular structures of proteins. Extensive use is made of modern computational methods to analyze the structures and their dynamics.

One research effort is directed toward elucidating the precise molecular mechanisms of the regulation of muscle contraction. The proteins which are involved in the regulatory process have been identified and include: tropomyosin, a highly helical molecule that forms filaments wound around actin, and troponin, a complex consisting of three polypeptide chains, that binds to tropomyosin. Detailed information about the structure of these proteins is necessary before their roles in regulation can be understood. We are also interested in the recognition of calcium by muscle proteins, and have studied mutants of parvalbumin to dissect the physical chemical principles involved in calcium signalling. The technique best suited for obtaining this information is X-ray crystallography.

Another project we have underway is directed towards obtaining an atomic description of the basis for binding of oxygen and other ligands to myoglobin. Detailed three-dimensional structures are being determined for native and mutant myoglobins with various ligands bound to the protein. We are moving towards a quantitative understanding of the engineering of heme proteins. The work is being extended to hemoglobin as potential cell-free blood substitute.

Organisms have proteins that are highly adapted to the growing conditions in the environment. We have determined structures of enzymes from hyperthermophilic bacteria to reveal aspects of the connections of protein structure to dynamics, which is an integral part of proteins' designs.

We are also working to develop new techniques for observing the dynamics of proteins and nucleic acids using diffuse X-ray scattering analysis and molecular dynamics simulations. The result will be a transition from "snapshots" of macromolecules to the generation of "movies" of molecules in action.

A new direction in our studies includes computational biology. In particular, the use of modern algorithms from computer science and applied mathematics to solve interesting biological problems.



    

 

 

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