We will review the structure of proteins, nucleic acids, carbohydrates, lipids, and the forces and interactions maintaining their structure in solution. We will describe the thermodynamics and kinetics of protein folding. The principles of polymer chain statistics and of helix-coil transitions in biopolymers will be reviewed next, together with biopolymer dynamics. We will then cover the main structural methods in biology: X-ray crystallography, MNR and fluorescence spectroscopy, electron and probe microscopy, and single molecular methods.

We will review the molecular driving forces that determine the structure and function of proteins and nucleic acids, and then describe how concepts of thermodynamic equilibrium and the competition between energy and entropy help us solve biological problems at the molecular level, such as ligand-receptor binding, conformational flexibility of DNA, and protein folding. We will then develop analytical models for bacterial chemotaxis, swimming of sperm, stepping of molecular motors, neuronal firing, vision, and photosynthesis. The course will also introduce advanced biophysical methods, such as single-molecule imaging and manipulation, and electrophysiology.

Hours and Workload Expectation
3 hours of instructor presentation of course materials and 1-hour discussion per week, 5 hours of outside work hours per week. There will will a midterm, final exam, student presentations and homework.

Repeat Rules

Course is not repeatable for credit.

Requirements class fulfills