作者: Hoi Sung Chung , Ali Shandiz , Tobin R. Sosnick , Andrei Tokmakoff
DOI: 10.1021/BI801603E
关键词: Equilibrium unfolding 、 Chemical physics 、 Temperature jump 、 Protein folding 、 Folding (chemistry) 、 Phi value analysis 、 Crystallography 、 Microsecond 、 Nanosecond 、 Chemistry 、 Phase (matter)
摘要: Crucial to revealing mechanistic details of protein folding is a characterization the transition state ensemble and its structural dynamics. To probe ubiquitin thermal unfolding, we examine unfolding dynamics kinetics wild-type mutant using time-resolved nonlinear infrared spectroscopy after nanosecond temperature jump. We observe spectral changes on two different time scales. A fast nonexponential microsecond phase attributed downhill from region, which induced by shift barrier due rapid change. Slow millisecond arise thermally activated kinetics. Mutants that stabilize or destabilize β strands III−V lead decreased increased amplitude phase, indicating disruption weakening these occurs in state. Unfolding features microseconds milliseconds can be explained temperature-dependent c...