Fall, every year
Course Director:
Kim Sharp, Ph.D., sharpk@mail.med.upenn.edu
This course introduces students to the physical and chemical properties of proteins, nucleic acids, and membranes. The emphasis in BMB 508 is on thermodynamics and structure, with several lectures devoted to the biophysical methods used to study biological macromolecules. This is intended to be a first course for graduate students with an undergraduate background in physics, chemistry, or biology.
Required Texts (in stock at Penn Bookstore):
Cantor & Schimmel, Biophysical Chemistry Part 2: Techniques for the Study of Biological Structure and Function, Freeman & Co.
van Holde, Johnson, & Ho,Principles of Physical Biochemistry, 2nd Edition, Prentice Hall.
Sample outline:
| Lecture | Topic |
| 1 | Introduction/Molecular interactions |
| 2 | Molecular interactions |
| 3 | Molecular interactions |
| 4 | Ligand Binding |
| 5 | Denaturation, Folding |
| 6 | Calorimetry |
| 7 | Sedimentation |
| 8 | NMR Spectroscopy |
| 9 | NMR Spectroscopy |
| 10 | NMR Spectroscopy |
| 11 | EPR Spectroscopy |
| 12 | Spectroscopic probes |
| 13 | Spectroscopic probes |
| Mid-term Examination |
| 14 | Optical imaging |
| 15 | Magnetic Resonance Imaging |
| 16 | X-ray Diffraction |
| 17 | X-ray Diffraction |
| 18 | Molecular analysis - modeling |
| 19 | Protein Structure |
| 20 | Protein Structure |
| 21 | Nucleic Acids Structure |
| No class |
| 22 | High order structure, electron microscopy |
| 23 | Scattering methods |
| 24 | Protein chemistry |
| 25 | Protein design & engineering |
| 26 | Protein design & engineering |
| Final Examination |