Terminal sidechain packing of a designed beta-hairpin influences conformation and stability.

ABSTRACT: While end capping in alpha-helices is well understood, the concept of capping a beta-hairpin is a relatively recent development; to date, favorable Coulombic interactions are the only example of sidechains at the termini influencing the overall stability of a beta-hairpin. While cross-strand hydrophobic residues generally provide hairpin stabilization, particular when flanking the turn region, those remote from this location appear to provide little stabilization. While probing for an optimal residue at a hydrogen bond position near the terminus of a designed beta-hairpin a conservative, hydrophobic, V --> I mutation was observed to not only result in a significant change in fold population but also effected major changes in the structuring shifts at numerous sites in the peptide. Mutation

SUBMITTER: Eidenschink L 

PROVIDER: S-EPMC3159043 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature