BCH 612 Structure and Function of Proteins and Enzymes
Syllabus - Fall, 2013
Instructors / Office / Phone / EmailHaining Zhu (Course Director) / 165 BBSRB / 3-3643 /
Luke Bradley / MN222 Med. Sci. Bldg. / 3-1826 /
Louis Hersh / 261 BBSRB / 3-5549 /
Harry LeVine III / 209 Sanders Brown / 7-1412x224 /
Konstantin V. Korotkov / 267 BBSRB / 3-5493 /
Qingjun Wang / 163 BBSRB / 3-5335 /
Time:10:00 - 11:15am, Tuesday and Thursday (unless noted otherwise).
Place:BBSRB, Rm 231 (unless noted otherwise).
This course is designed to provide the student with an appreciation of the factors that govern the behavior of protein molecules and information concerning how protein molecules are studied. The course will concentrate on aspects of protein expression and purification, protein structure and its determination, principles of protein folding and three dimensional structure, and mechanisms of protein action, catalysis and regulation. Emphasis will be placed on experiments and methodology employed to study proteins.
This will be a lecture course and will be graded on the basis of three exams of equal weighting. They will consist of essay and problem solving questions graded as objectively as possible on a numerical scale.
Grade / Numerical ScoreA / 90-100% (or > average + 1x S.D.)
B / 80-89% (or > average – 0.5x S.D.)
C / 70-79% (or > average – 1.5x S.D.)
Graduate students cannot receive a grade of D, hence any score below 70% (or < average – 1.5x S.D.) will be classified as an E.
There will not be a textbook for the course. References from the scientific literature covering specific topics will be provided for the material presented in the class. Participants are required to read these references as a supplement to the lectures. A number of standard resources and texts will be recommended for more general information.
Last year’s students commented that there weren’t enough coverage on protein functions. How should we address this?
Date / Topic / InstructorThu. Aug. 28 / 1. Introduction to course and review of basic concepts. / Zhu
I’m thinking about adding 1-2 lectures here about general concepts about protein folding, structure and function.
Tues. Sept. 2 / 2. Protein expression: current approaches to protein expression in bacterial host systems, vectors; PCR etc. / Hersh
Thu. Sept. 4 / 3. Protein expression: mammalian, insect and viral systems. / Hersh
Tu. Sept. 9 / 4. Protein purification: basic concepts and approaches. / Hersh
Thu. Sept. 11 / 5. Protein purification: modern approaches. / Hersh
Tues. Sept. 16 / 6. Spectroscopic methods for studying proteins (I): UV/vis & circular dichroism / Wang
Thu. Sept. 18 / 7. Spectroscopic methods for studying proteins (II): fluorescence & chemiluminescence / Wang
Tues. Sept. 23 / 8. Fluorescence microscopy: basics. / Wang
Thu. Sept. 25 / 9. Fluorescence microscopy: advanced topics. / Wang
Tues. Sept. 30 / 10. Laboratory demonstration of spectroscopic and microscopic techniques.How do students like this lab demo? Should we keep this? / Wang
Thu. Oct. 2 / 1st Exam (lectures 1-10) (regular time 10-11:15, B202)
Tues. Oct. 7 / 11. Site-directed mutagenesis. / Bradley
Thu. Oct. 9 / 12. Library screens and selection, an overview. / Bradley
Tues. Oct. 14 / 13. Principles and energetics of protein folding and stability. / Korotkov
Thu. Oct. 16 / 14. Principles and energetics of protein folding and stability. / Korotkov
Tues. Oct. 21 / 15. Protein stability: differential scanning calorimetry and other biophysical techniques. / Korotkov
Thu. Oct. 23 / 16. Ligand binding: isothermal titration calorimetry and fluorescence techniques. / Korotkov
Tues. Oct. 28 / 17. Introduction to protein X-ray crystallography and NMR spectroscopy.
Konstatin: You can re-organize these lectures to cover what you think are important for biochemistry Ph.D. students. / Korotkov
Thu. Oct. 30 / 18. Principles of protein mis-folding / LeVine
Tues. Nov. 4 / 19. Cellular responses to proteins behaving badly / LeVine
Thu. Nov. 6 / 20. Physical methods for the study of protein misfolding / LeVine
Tues. Nov. 11 / 21. Current approaches to modeling protein misfolding diseases / LeVine
Tues. Nov. 13 / 2nd Exam (lectures 11-21) (regular time 10-11:15, B202)
Tues. Nov. 18 / 22. Protein post-translational modifications. / ????
Thu. Nov. 20 / 23. Protein post-translational modifications.
Here’s another opportunity to add protein function regulation by modifications. / ????
Tues. Nov. 25 / 24. Proteomics: principles of mass spectrometry. / Zhu
Thu. Nov. 27 / Thanksgiving (no class) / -
Tues. Dec. 2 / 25. Proteomics: application of mass spectrometry. / Zhu
Thu. Dec. 4 / 26. Proteomics: other approaches. / Zhu
Tues. Dec. 9 / 27. Proteomics: laboratory demonstration. / Zhu
Thu. Dec. 11 / Flexible Day / Zhu
Finals Week / Final (3rd) Exam (lectures 21-27)
Tuesday 12/16, 10am-12noon, B202
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