The role of aromatic residues in the hydrophobic core of the villin headpiece subdomain.

ABSTRACT: Small autonomously folding proteins are of interest as model systems to study protein folding, as the same molecule can be used for both experimental and computational approaches. The question remains as to how well these minimized peptide model systems represent larger native proteins. For example, is the core of a minimized protein tolerant to mutation like larger proteins are? Also, do minimized proteins use special strategies for specifying and stabilizing their folded structure? Here we examine these questions in the 35-residue autonomously folding villin headpiece subdomain (VHP subdomain). Specifically, we focus on a cluster of three conserved phenylalanine (F) residues F47, F51, and F58, that form most of the hydrophobic core. These three residues are oriented such that they may pr

SUBMITTER: Frank BS 

PROVIDER: S-EPMC2373478 | biostudies-literature | 2002 Mar

REPOSITORIES: biostudies-literature