Complex kinetics and residual structure in the thermal unfolding of yeast triosephosphate isomerase.

ABSTRACT:

Background

Saccharomyces cerevisiae triosephosphate isomerase (yTIM) is a dimeric protein that shows noncoincident unfolding and refolding transitions (hysteresis) in temperature scans, a phenomenon indicative of the slow forward and backward reactions of the native-unfolded process. Thermal unfolding scans suggest that no stable intermediates appear in the unfolding of yTIM. However, reported evidence points to the presence of residual structure in the denatured monomer at high temperature.

Results

Thermally denatured yTIM showed a clear trend towards the formation of aggregation-prone, β-strand-like residual structure when pH decreased from 8.0 to 6.0, even though thermal unfolding profiles retained a simple monophasic appearance regardless of pH. However, kinetic studies

SUBMITTER: Labastida-Polito A 

PROVIDER: S-EPMC4558838 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature