Education and Training
B.A., Williams College
M.S. and Ph.D., University of California, San Diego
NIH Post-doctoral fellow, University of Pennsylvania
Vibrational spectroscopy and conformational flexibility: My main research interest is the development of new physical techniques for understanding conformational flexibility and structural switching in proteins. The main instrumental techniques employed in my laboratory are infrared absorption spectroscopy and Raman scattering. My group uses the vibrational bands of both natural and unnatural amino acids to determine the residue-level structural distribution of proteins with particularly dynamic structures. We also use molecular dynamics simulations and frequency calculations to provide a computational picture of what our experimental data shows about protein structures.
Conformational flexibility is intrinsic to a protein’s ability to function; if proteins were not floppy, they couldn’t do anything! For enzymes, flexibility allows them to capture, convert and release specific chemical targets. For proteins that are building blocks in larger structures, the ability of the building blocks to adopt multiple shapes can allow the construction of complex biomolecular assemblies. Vibrational spectroscopy is uniquely suited to observation of structural distributions, rather than just average protein structures. The techniques developed in my laboratory have been applied to understand molecular flexibility, interactions between proteins and other molecules, and self-assembly behavior in complexes made from multiple proteins. Biological systems of interest for us include regulatory proteins, membrane-associated proteins, bacteriosynthetic proteins, viral protein complexes, and aggregating peptides and proteins.