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Biochem 651 - Introduction to modern biochemical laboratory techniques.
Fall 2009-2010
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Course Materials |
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Course Description:
Section 001
(Class Number: 70532
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| Instructor(s): |
Fox,Brian G.; Gillian,Anne Lynn; Senes,Alessandro |
| TA(s): |
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| Credits: |
2
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| Day: |
MWF
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Time: |
12:05 PM - 12:55 PM
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| Location: |
184 Russell Labs
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Website: |
http://www.biochem.wisc.edu/courses/biochem651/
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Description:
Students currently enrolled in Biochem 651:
Please find the complete course syllabus and course materials on Learn@UW.
BIOCHEMISTRY 651, Biochemical Methods, is an integrated lecture and lab course covering basic theories and techniques used in the experimental life sciences. The course is directed at upper level undergraduate majors in Biochemistry. Participants will learn how to apply a broad range of biochemical, genetic, and physical techniques to modern biochemical research.
Lectures are scheduled such that theoretical and practical aspects are introduced before the corresponding lab experiments. The laboratory experiments are designed to provide "hands-on" experience with instruments and techniques that are frequently used in both biochemical and clinical research. These experiments focus on instrumental techniques including spectrophotometry, gel electrophoresis, enzyme assays, and protein purification. Students will begin the course by PCR amplifying and cloning the bacterial lac z gene. As the semester progresses the lac z clone will be used to over express β-galactosidase which will then be purified and assayed for functionality. The lab reports will be graded on the basis of data collection and analysis, and on their clarity, accuracy, and detail.
Two exams will cover the lecture materials and related lab experiments, and will contain both multiple choice and short essay questions.
Lectures and Laboratory Experiments:
- Amplification of a DNA segment by PCR
- Molecular cloning of the lac z gene
- Analytical electrophoresis of proteins and nucleic acid
- UV-visible spectrometry and spectroscopy in biochemical research
- Assays to monitor enzyme activity
- Affinity purification of over expressed protein
Discussions/Labs/Other:
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LAB - 301
(Class Number: 70552
)
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| Instructor(s): |
Fox,Brian G.; Gillian,Anne Lynn; Senes,Alessandro |
| TA(s): |
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| Credits: |
2
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| Day: |
M
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| Time: |
01:20 PM - 05:00 PM
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| Location: |
2145 MBS
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LAB - 302
(Class Number: 70553
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| Instructor(s): |
Fox,Brian G.; Gillian,Anne Lynn; Senes,Alessandro |
| TA(s): |
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| Credits: |
2
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| Day: |
T
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| Time: |
09:55 AM - 01:35 PM
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| Location: |
Rm 2145 MSB
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LAB - 303
(Class Number: 71646
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| Instructor(s): |
Fox,Brian G.; Gillian,Anne Lynn; Senes,Alessandro |
| TA(s): |
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| Credits: |
2
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| Day: |
W
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| Time: |
01:20 PM - 05:00 PM
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| Location: |
Rm 2145 MSB
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This portion of the course website has been secured. Please login
above to view. If you are logged in and still can't view anything, you don't
appear on our roster. Please contact the professor to add you to the course
roster.
Lab
Lab Orientation and General Laboratory Procedures
SPY
:
A Spectrophotometric Study of Hemoglobin
EZA
: Development of an Enzyme Assay
ING: Introduction
ING-Part 1:
Induction, Sampling, Growth Measurements
ING-Part 2:
Enzyme Assays plus Denaturing Polyacrylamide Gel Electrophoresis
MBL: Cloning the lux operon from Vibrio fischeri
MBL-Part 1: Isolation of Genomic DNA from V. fischeri
MBL-Part 2: Spectrophotometric Analysis of Genomic and Plasmid DNA
MBL-Part 3: Restriction Digestion of Genomic and Plasmid DNA
MBL-Part 4: Quantitation of DNA by Plate Fluorescence and Agarose Gel Electrophoresis
MBL-Part 5: Ligation of Genomic DNA Restriction Fragments to Vector
MBL-Part 6: Transformation of Competent Escherichia coli DH5¿
MBL-Part 7: Identification and Isolation of Bioluminescent Clones
MBL-Part 8: Plasmid Mini-preps From Lux+ Clones and Restriction
Digestion and Agarose Electrophoresis of Plasmids
MBL-Part 9: Summary
GPC
: Gel Permeation Chromatography of Egg White Protein
Buffer Appendices
General topic reading list
The assigned readings will come from the following:
Principles of Biochemistry, 4th ed., Nelson, D. L. and Cox, M. M. (2004) New York, Worth Publishing.
Supplemental readings come from these, which can be found at Steenbock Library.
1. Ninfa, A.J. and Ballou, D.P. (1999) Fundamental Laboratory Approaches for Biochemistry and Biotechnology. Fitzgerald Scientific Press, Inc.
2. Branden, C. and Tooze, J. (1991) Introduction to Protein Structure, New York, Garland Publishing.
3. Brock, T. D., Madigan, M. T., Martinko, J. M., and Parker, J. (1994) Biology of Microorganisms, 7th ed., Englewood Cliffs, Prentice Hall.
4. Cooper, T. G. (1977) Tools of Biochemistry, New York, John Wiley and Sons.
5. Creighton, T. E. (1994) Proteins: Structure and Molecular Properties, 2nd ed., New York, W. H. Freeman.
6. Deutscher, M. (1991). Guide to Protein Purification. Methods Enzymol., 182, 1-894.
7. Harris, D. C. (1998, 2003) Quantitative Chemical Analysis, 4th ed., New York, W. H. Freeman.
8. Robyt, J. F. and White, B. J. (1987) Biochemical Techniques: Theory and Practice, Chicago, Waveland Press.
9. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning, A Laboratory Manual, 2nd ed., Cold Spring Harbor, Cold Spring Harbor Laboratory Press.
10. Scopes, R. K. (1994) Protein Purification: Principles and Practice, 3rd ed., New York, Springer-Verlag.
11. Skoog, D. A. and Leary, J. J. (1992) Principles of Instrumental Analysis, 3rd ed., New York, Saunders College Publishing.
Guidelines for preparation of lab reports
1. For each experiment, each student should prepare their own lab report, including plots, data analysis, and answers to questions. You may discuss how to best answer the questions and how to perform sample calculations with other students.
It is absolutely not acceptable for a group of students to print out multiple copies of a joint report for grading purposes.
Please also note that simple rearrangements of clauses and minor phrases that maintain the same overall structure and content can be considered plagarism in some contexts and should be avoided.
The best strategy is to prepare your final written statements independently after discussions are complete.
2. As discussed in class, lab reports should be printed from word processing software or should be typewritten. The report should be prepared with 2.5 cm margins on all sides in a 12 point font such Times Roman, and double line spacing should be used.
Handwritten or other unformatted reports will be considered late and will be returned for revision. Handwritten labels may be used on gels, spectra, and other primary data materials, and complicated equations may be handwritten, however.
3. Correct punctuation, correct spelling, and the use of complete sentences will be expected, and reports that significantly deviate from normal usage will receive deductions in point totals.
4. Answers to questions should be clearly identified by number, and the graders will most appreciate a short, to-the-point answer. In this regard, consider the following quote by the (in)famous author Oscar Wilde
"I would have written a shorter letter, but I didn't have the time."
A short, well-structured answer takes more thought and revision than a stream-of-consciousness deposition. The graders in Biochemistry 651 will be looking for short, well-structured answers.
How to Insert Equations in Microsoft Word
Click here for Jenna's Instructions
No homework assignments are currently due.
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