A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain.

ABSTRACT: Many small proteins fold highly cooperatively in an all-or-none fashion and thus their native states are well protected from thermal fluctuations by an extensive network of interactions across the folded structure. Because protein structures are stabilized by local and nonlocal interactions among distal residues, dissecting individual substructures from the context of folded proteins results in large destabilization and loss of unique three-dimensional structure. Thus, mini-protein substructures can only rarely be derived from natural templates. Here, we describe a compact native 24-residues-long supersecondary structure derived from the hyperstable villin headpiece subdomain consisting of helices 2 and 3 (HP24). Using a combination of experimental techniques, including NMR and small-angle

SUBMITTER: Hocking HG 

PROVIDER: S-EPMC4317555 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature