Proteins are large biological molecules that control the majority of biological function. The way that a given protein does this is determined in part by the arrangements of its atoms in space (its structure) and by the way that it moves and its bonds and atoms wiggle (its dynamics). Both of these characteristics are influenced by a combination of intramolecular forces (hydrogen-bonding, hydrophobic effects, steric hindrance, electrostatics) and intermolecular forces (protein-protein or protein-ligand interactions, and solvent environment effects), all of which can influence the energy and entropy of a protein or complex. This is important because ultimately all biological processes come down to a balance between maximizing entropy and minimizing energy.

My research program seeks to describe how these physical forces influence the structure and motions of proteins and peptides. Students in my group are currently using NMR spectroscopy to investigate the hydrogen-bonding networks in a variety of small, hydrophobic, helical peptides using H/D exchange kinetics. Also, in a collaboration with Robert Oswald at Cornell University, we are studying the dynamic motions of signal transduction proteins and the interplay between energy and entropy in protein-ligand binding events using multidimensional NMR spectroscopy. Details on these projects, as well as complete presentations made by undergraduate researchers can be viewed by clicking on the menu tabs on the left or the text links below.