Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE.

ABSTRACT: Most proteins are in equilibrium with partially and globally unfolded conformations. In contrast, kinetically stable proteins (KSPs) are trapped by an energy barrier in a specific state, unable to transiently sample other conformations. Among many potential roles, it appears that kinetic stability (KS) is a feature used by nature to allow proteins to maintain activity under harsh conditions and to preserve the structure of proteins that are prone to misfolding. The biological and pathological significance of KS remains poorly understood because of the lack of simple experimental methods to identify this property and its infrequent occurrence in proteins. Based on our previous correlation between KS and a protein's resistance to the denaturing detergent SDS, we show here the application of

SUBMITTER: Xia K 

PROVIDER: S-EPMC2077256 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature