Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.

ABSTRACT: Understanding the interconversion between thermodynamically distinguishable states present in a protein folding pathway provides not only the kinetics and energetics of protein folding but also insights into the functional roles of these states in biological systems. The protein component of the bacterial RNase P holoenzyme from Bacillus subtilis (P protein) was previously shown to be unfolded in the absence of its cognate RNA or other anionic ligands. P protein was used in this study as a model system to explore general features of intrinsically disordered protein (IDP) folding mechanisms. The use of trimethylamine N-oxide (TMAO), an osmolyte that stabilizes the unliganded folded form of the protein, enabled us to study the folding process of P protein in the absence of ligand. Transient

SUBMITTER: Chang YC 

PROVIDER: S-EPMC2937257 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature