Biophysical Chemistry

Catalog description

This three-credit course will cover the key theories and experimental methods of contemporary biophysics and biophysical chemistry. The course discusses the structures and dynamics of biomolecules (such as proteins, DNAs, and RNAs), the statistical mechanical models to describe the behaviors of biopolymers and the biophysical methods to analyze the structures of biopolymers in solution, the biophysical theories for protein folding/unfolding and the experimental methods to measure the kinetics of protein folding/unfolding and the protein structural dynamics, the principles of biomolecule structure determination by X-ray crystallography and cryogenic electron microscopy, and fluorescence microscopes, as well as the theories to describe ligand binding to biological macromolecules (such as receptors, protein complexes, aptamers, etc.) and the experimental methods to measure ligand binding. For all the topics covered by this course, emphasis will be laid on both theoretical models and experimental methods will be discussed. Classic and modern biophysical and biochemical techniques ranging from spectroscopy and FRET to optical microscopy, including super-resolution and micromanipulation techniques, will be covered. Applications of these biophysical techniques will also be discussed.