Modeling transient collapsed states of an unfolded protein to provide insights into early folding events.

ABSTRACT: The primary driving force for protein folding is the sequestration of hydrophobic side chains from solvent water, but the means whereby the amino acid sequence directs the folding process to form the correct final folded state is not well understood. Measurements of NMR line broadening in spin-labeled samples of unfolded apomyoglobin at pH 2.3 have been used to derive a quantitative model for transient hydrophobic interactions between various sites in the polypeptide chain, as would occur during the initiation of protein folding. Local clusters of residues with high values for the parameter "average area buried upon folding" (AABUF) form foci not only for local contacts but for long-range interactions, the relative frequencies of which can be understood in terms of differences in the exten

SUBMITTER: Felitsky DJ 

PROVIDER: S-EPMC2359776 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature