The unfolded state of the villin headpiece helical subdomain: computational studies of the role of locally stabilized structure.

ABSTRACT: The 36 residue villin headpiece helical subdomain (HP36) is one of the fastest cooperatively folding proteins, folding on the microsecond timescale. HP36's simple three helix topology, fast folding and small size have made it an attractive model system for computational and experimental studies of protein folding. Recent experimental studies have explored the denatured state of HP36 using fragment analysis coupled with relatively low-resolution spectroscopic techniques. These studies have shown that there is apparently only a small tendency to form locally stabilized secondary structure. Here, we complement the experimental studies by using replica exchange molecular dynamics with explicit solvent to investigate the structural features of these peptide models of unfolded HP36. To ensure co

SUBMITTER: Wickstrom L 

PROVIDER: S-EPMC4805113 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature