The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structure.

ABSTRACT: Cold denaturation is a general property of globular proteins, and the process provides insight into the origins of the cooperativity of protein folding and the nature of partially folded states. Unfortunately, studies of protein cold denaturation have been hindered by the fact that the cold denatured state is normally difficult to access experimentally. Special conditions such as addition of high concentrations of denaturant, encapsulation into reverse micelles, the formation of emulsified solutions, high pressure, or extremes of pH have been applied, but these can perturb the unfolded state of proteins. The cold denatured state of the C-terminal domain of the ribosomal protein L9 can be populated under native-like conditions by taking advantage of a destabilizing point mutation which lead

SUBMITTER: Shan B 

PROVIDER: S-EPMC3319020 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature