Take me to the Fall Term '99 Time Schedule for Biophysics.
Prerequisites & Distribution: Chem. 463, Biol. Chem. 415, or Chem 420; permission of course director. (3). (Excl). (BS).
Course Homepage: No Homepage Submitted.
This course is the first of a two-term Biophysical Chemistry series 520/521, but it can be taken as stand-alone course as well. The course offers an overview of protein, nucleic acid, lipid and carbohydrate structures. Intra- and inter-molecular forces, helix-coil transitions, and protein folding will be treated in a thermodynamical context. Thermodynamics of solutions, configurational statistics, ligand interactions, multi-site interactions, and cooperativity are treated in depth. Kinetics of protein-ligand binding, including electron transfer and ligand diffusion are discussed. Chemistry 520 will introduce and explain the physicochemical properties of biological macromolecules and their complexes, mostly in solution.
Currently, biophysical, biochemical and pharmaco-chemical research literature is full with papers interpreting the properties of biological macromolecules on the the basis of their three-dimensional structure. This course will expand on that concept by offering a rigorous background in energetics, folding, interactions, and dynamics. As such the course is important to any student who has to deal with the concepts of biomolecular function and structure such as biochemists, biophysicists, mathematical biologists, and molecular pharmacologists. This course will also serve as a basis for the graduate student who will be specializing in any of these topics for thesis research. Molecular dynamics will be introduced. Instructional material: Cantor and Shimmel, Biophysical Chemistry, Part I and III and Creighton, Proteins, Structures and Molecular Properties. Evaluation: homework (50%), midterm exam (20%) and final exam (30%).
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