β-Bulge triggers route-switching on the functional landscape of interleukin-1β.

ABSTRACT: Proteins fold into three-dimensional structures in a funneled energy landscape. This landscape is also used for functional activity. Frustration in this landscape can arise from the competing evolutionary pressures of biological function and reliable folding. Thus, the ensemble of partially folded states can populate multiple routes on this journey to the native state. Although protein folding kinetics experiments have shown the presence of such routes for several proteins, there has been sparse information about the structural diversity of these routes. In addition, why a given protein populates a particular route more often than another protein of similar structure and sequence is not clear. Whereas multiple routes are observed in theoretical studies on the folding of interleukin-1β (IL-

SUBMITTER: Capraro DT 

PROVIDER: S-EPMC3277114 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature