B.A., Williams College
M.S. and Ph.D., University of California, San Diego
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 at the atomic level. The main instrumental techniques employed in my laboratory are infrared absorption spectroscopy and Raman scattering. We use the vibrational bands of modified amino acids to determine the residue-level structural distribution of proteins with particularly dynamic 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 will be applied to understand the relationship between molecular flexibility and self-assembly behavior in complexes made from multiple proteins: for example, viral capsids and β-aggregates.