Probing the folding intermediate of Bacillus subtilis RNase P protein by nuclear magnetic resonance.

ABSTRACT: Protein folding intermediates are often imperative for overall folding processes and consequent biological functions. However, the low population and transient nature of the intermediate states often hinder their biochemical and biophysical characterization. Previous studies have demonstrated that Bacillus subtilis ribonuclease P protein (P protein) is conformationally heterogeneous and folds with multiphasic kinetics, indicating the presence of an equilibrium and kinetic intermediate in its folding mechanism. In this study, nuclear magnetic resonance (NMR) spectroscopy was used to study the ensemble corresponding to this intermediate (I). The results indicate that the N-terminal and C-terminal helical regions are mostly unfolded in I. 1H−15N heteronuclear single-quantum coherence NMR spec

SUBMITTER: Chang YC 

PROVIDER: S-EPMC3081390 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature