Nuclear magnetic resonance studies of denatured states of bovine pancreatic trypsin inhibitor.

摘要

Residual structure in denatured proteins is an important issue in understanding protein folding, stability, transport across biological membranes, and protein turnover in living organisms. This thesis has described the characterization of denatured states of bovine pancreatic trypsin inhibitor (BPTI) by high resolution nuclear magnetic resonance (NMR).;BPTI is a small globular protein of 58 amino acids with three disulfide bonds. Reduced BPTI (with all disulfides reduced to thiols) is unfolded; BPTI with one disulfide bridge is partially folded. In this work, chemically synthesized reduced BPTI ((R) ;2D ;Hydrodynamic measurements of denatured forms, made by pulsed-field gradient NMR (PFG NMR), provide information on the extent of collapse for denatured states. PFG NMR experiments show that reduced, unfolded BPTI is as compact as unfolded BPTI constrained by a disulfide crosslink.;