Effects of alternative side chain pairings and reverse turn sequences on antiparallel sheet structure in beta-peptide hairpins.
[structure: see text] We describe a series of beta-peptide hexamers that allow us to explore relationships between sequence and hairpin folding. Different reverse turn segments are compared at the central two positions, and the outer residues allow a variety of interstrand side chain-side chain pairings. NMR analysis in methanol demonstrates that several reverse turn and side chain pairing arrangements are compatible with antiparallel beta-peptide sheet structure; however, none of the beta-peptides folds in water.
Langenhan
Joseph M
JM
Department of Chemistry, University of Wisconsin, 1101 University Ave., Madison, Wisconsin 53706, USA.
Gellman
Samuel H
SH
D009682:Magnetic Resonance Spectroscopy; D000432:Methanol / Q000737:chemistry; D010455:Peptides; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D014867:Water / Q000737:chemistry
C447154:BH8 beta-hairpin peptide; D010455:Peptides; D011506:Proteins; D014867:Water; D000432:Methanol