Biophysics involves the application of physical techniques to achieve an understanding of life processes at a molecular level. Physical techniques are central to the measurement of the atomic structure, dynamics and interactions of molecules that are a core foundation of modern molecular biology, while physical theory governs the predicted behavior of biomolecules and helps us achieve a mechanistic understanding of how they work. Thus, biophysics is a central science in the fundamentals of normal physiology, molecular pathology, and in the development of pharmaceutical remedies for a wide range of diseases.
This is the second of two primarily lecture courses that will prepare graduate and advanced undergraduates for research and technical work in Molecular Biophysics. It will cover the practical aspects of the elucidation of macromolecular structure and dynamics by NMR spectroscopy and x-ray crystallography, and the characterization of macromolecular interactions by electron microscopy, mass spectrometry and fluorescence methods. It will examine computational methods for interpreting structure, predicting properties and simulating mechanisms of action.
At the conclusion of this course, students will have a working understanding of the primary experimental and computational methods by which the structure, dynamics and interactions of biomolecules are elucidated and their actions simulated. Students will be able to critically assess primary research literature written for a general scientific audience that uses any of the common physical approaches to understand macromolecular systems. Students will understand the nature of advances that can be made with the principal techniques and their limitations. They will also be prepared for mentored practical research investigations that use the primary methods.
| OHSU | PSU | |
| Course number | BCMB 631 (CRN 31377) | CH 510 (Sp. Topics/Biophysics; this ID to be replaced soon.) |
| Credit hours | 3 | 4 |
| Offered | Spring 2011 & annually thereafter | |
Introductory Biophysics or consent of the course directors.
The course will be team-taught by faculty from Portland State University and Oregon Health & Science University.
| OHSU | PSU | |
| Michael S. Chapman, Ph.D. | David H. Peyton, Ph.D. | |
| mailto:chapmami@ohsu.edu | mailto:peytond@pdx.edu | |
| Office hours | Mon noon-1pm; Wed 2-3pm: MRB 534A | TBA: 323B SB1 |
| Web URL | http://xtal.ohsu.edu/ | http://web.pdx.edu/~peytond/ |
| Phone | (503) 494-1025 | (503) 725-3875 |
Practical crystallography
Crystallization
Data collection
Phasing by molecular replacement
Model-building & refinement
Advanced NMR
Biomolecular structure determination
Dynamics
Paramagnetic NMR, ESR, spin-labeling & solid-state NMR
Microscopy
Light microscopy - Theory; Fluoresence, Confocal & Correlative
Electron microscopy Theory of transmission EM; Biological application
Tomography & 3D single-particle reconstruction
Analysis of structure
Databases & Homology modeling
Energy minimization; Poses & Docking
Electrostatics - potentials & pKs
Molecular Dynamics
Simulated Annealing
Normal modes
Enhanced sampling / acceleration
Mass Spectrometry
Theory & instrumentation
Footprinting & dynamics
Principles of Physical Biochemistry (2nd Ed.) by van Holde, K.E., Johnson, C. & Ho, P.S. (2006) Prentice Hall, ISBN-10: 0130464279 / ISBN-13: 9780130464279
In-class presentations will be posted at the discretion of the instructor following class with links from Schedule.
There will be one mid-term and a final examination each contributing ~50% to the overall assessment.