Biophysical chemistry studies the properties of biological molecules along with the principles and methods of physics and physical chemistry. Experimentation and computation combine at Cornell to probe the structure, dynamics, interactions and functions of individual biological macromolecules and supramolecular complexes. Primary biological conformational processes such as protein folding, protein dynamics and binding are addressed by theoretical methods and experiments. X-ray crystallography determines structures of biologically active molecules such as anti-tumor agents, immunosuppressants and protein complexes.
Fluorescence spectroscopy, microscopy, and flow cytometry measure ligand binding and the structural interactions of cell surface receptors and lipids critical for signal transduction during immune responses and carcinogenesis. Laser photolysis techniques are used to study electron transfer reactions and release photolabile ligands for triggering receptors in nerve cells. Electron spin resonance (ESR) spectroscopy allows investigation of the dynamics of membranes and protein-lipid interactions.
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