Center for Molecular Biophysics & Biophysical Chemistry

Jean S. Baum
Professor of Chemistry, Rutgers University
(732) 445-5666
Wright-Rieman Laboratories, Room 159

Our laboratory is interested in applying and developing NMR to study important problems in biophysical chemistry. The first problem that we are investigating is the mechanism of protein folding. Characterization of the folding processes of proteins is important to understand the determinants of protein structure and function. We are using a number of NMR approaches to characterize folding intermediates in structural and kinetic terms. One approach of the laboratory is to study the conformation of denatured, and partially folded proteins such as the molten globule state of alpha-lactabumin. A second and complementary NMR approach is to apply "real-time" kinetics to the folding of proteins. We are developing approaches to study real time NMR folding and applying these to model peptides of the collagen triple helix.

Our second major research effort is to use NMR to define the molecular basis of recognition. We are approaching this problem from a number of directions. One approach is to study recognition regions in triple helical domains with repeating (X-Y-Gly)n sequences. The rod-like extended domains formed by the triple helices play an important structural role, and within these domains, specific sequences bind a variety of biological macromolecules, such as fibronectin and cell surface integrins. A second approach to studying recognition is to investigate the complex of a catalytic fragment of leukemia virus reverse transcriptase with nucleic acid.