Slow conformational changes in the rigid and highly stable chymotrypsin inhibitor 2.

ABSTRACT: Slow conformational changes are often directly linked to protein function. It is however less clear how such processes may perturb the overall folding stability of a protein. We previously found that the stabilizing double mutant L49I/I57V in the small protein chymotrypsin inhibitor 2 from barley led to distributed increased nanosecond and faster dynamics. Here we asked what effects the L49I and I57V substitutions, either individually or together, have on the slow conformational dynamics of CI2. We used ¹⁵ N CPMG spin relaxation dispersion experiments to measure the kinetics, thermodynamics, and structural changes associated with slow conformational change in CI2. These changes result in an excited state that is populated to 4.3% at 1°C. As the temperature is increased the popul

SUBMITTER: Gavrilov Y 

PROVIDER: S-EPMC10031225 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature