We have used simulated annealing methods developed at CABM to homology model this protein, and a manuscript describing this predicted structure is now in press. Nuclear relaxation time measurements are used to characterize intramolecular motion in these small proteins. Together with Dr. Levy, we have also developed a novel method for graphical analysis of nuclear relaxation data. This research has important implications in the fields of protein physical chemistry, molecular design, receptor-ligand interactions, protein folding, and oncogenesis. This protein-RNA interaction appears to be critical in allowing bacterial cells to acclimate to cold stress.
Serine proteases play critical roles in the physiology of blood.
A paper describing this work has been submitted for publication. Mechanisms by which proteins fold into their biologically-active conformations . A crucial area in the field of molecular biophysics involves determining how protein sequences fold into unique three-dimensional structures. We have made some efforts to understand protein folding mechanisms by analysis of three-dimensional structures of protein folding intermediates. These analyses provide important information about the sequential order of native structure formation in this folding process and about the role of structural dynamics in the energetics of folding.