Effect of subdomain interactions on methyl group dynamics in the hydrophobic core of villin headpiece protein.

ABSTRACT: Thermostable villin headpiece protein (HP67) consists of the N-terminal subdomain (residues 10-41) and the autonomously folding C-terminal subdomain (residues 42-76) which pack against each other to form a structure with a unified hydrophobic core. The X-ray structures of the isolated C-terminal subdomain (HP36) and its counterpart in HP67 are very similar for the hydrophobic core residues. However, fine rearrangements of the free energy landscape are expected to occur because of the interactions between the two subdomains. We detect and characterize these changes by comparing the µs-ms time scale dynamics of the methyl-bearing side chains in isolated HP36 and in HP67. Specifically, we probe three hydrophobic side chains at the interface of the two subdomains (L42, V50, and L75) as well as

SUBMITTER: Vugmeyster L 

PROVIDER: S-EPMC3926740 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature