This course is the first of a two-term Biophysical Chemistry series BIOPHYS 520/521, but it can be taken as stand-alone course as well. BIOPHYS 520 will introduce and explain the physicochemical properties of biological macromolecules and their complexes, mostly in solution. The course offers an overview of protein and nucleic acid 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 and thermodynamics of protein-ligand binding are discussed. The role of dynamics in protein function is introduced.
Currently, biophysical, biochemical, and pharmacochemical research literature is full with papers interpreting the properties of biological macromolecules on 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, molecular 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.
Instructional material: Dill & Bromberg, Molecular Driving Forces, 2003 and course packs.
Evaluation: homework (40%), midterm exam (30%) and final exam (30%).