Structural Biology, Biochemistry and Biophysics Faculty:
Nathan Alder, Associate Professor; Ph.D.: Analysis of the structure, function, and biogenesis of membrane proteins using multiple techniques, primarily fluorescence spectroscopy, and employing yeast as a model system; mitochondrial protein trafficking and assembly; high-resolution fluorescence-based mapping of membrane proteins and analysis of conformational dynamics.
Andrei Alexandrescu, Professor; Ph.D.: High-resolution solution NMR investigations of protein structure, folding, dynamics, and association; NMR methods to investigate residual structure in protein folding intermediates; conserved folding mechanisms of proteins that share the OB-fold structural motif; evolution of protein structure; structures of neuromuscular junction components; NMR methods to study amyloid fibrils; computational approaches to protein folding.
James Cole, Professor; Ph.D.: Analysis of macromolecular interactions using analytical ultracentrifugation and multiple biophysical techniques. The systems that we study include the RNA activated protein kinase (PKR); innate immunity antiviral defense pathway; RIG-I-like receptors.
Eric May, Assistant Professor; Ph.D.: Research in the May lab is focused on molecular, multi-scale and coarse-grained modeling of biological systems, wia th particular focus on viruses. Much of our research is related to understanding conformational changes of viral proteins induced by environmental factors or ligand binding. We also have an interest in understanding the mechanical/material properties of biological systems, particularly as it relates to single-molecule experiments and the development of biological nanomaterials.
Victoria Robinson, Associate Professor; Ph.D.: High-resolution determination of protein structures by X-ray crystallography. The goal of my research is to use genetic, biochemical and structural methodologies to study novel families of bacterial GTPases, which are potential targets for antimicrobial development.
Carolyn Teschke, Professor; Ph.D.: Biochemical, biophysical, and mutational analysis of virus assembly, especially of the thermodynamics of capsid assembly and maturation reactions.
– The role of the two SecA homologs in protein export in Mycobacterium tuberculosis.
– Protein folding in vivo and in vitro. Interaction of folding intermediates with molecular chaperones.
Simon White, Assistant Professor; Ph.D.: Research in the White lab is focused on the mechanism of assembly of RNA viruses. In particular, the Picornaviridae encompass many important human and animal pathogens, such as polio, foot and mouth disease, and the common cold.
Arlene Albert, Professor Emeritus, Ph.D.: The effect of lipids on the structure and function of membrane proteins. Specifically, the structure of the G-protein receptor, rhodopsin, its interaction with lipids and the role which the lipid bilayer composition plays in modulating the biochemistry of visual signal transduction.