Length-dependent stability and strand length limits in antiparallel beta -sheet secondary structure.

ABSTRACT: Designed peptides that fold autonomously to specific conformations in aqueous solution are useful for elucidating protein secondary structural preferences. For example, autonomously folding model systems have been essential for establishing the relationship between alpha-helix length and alpha-helix stability, which would be impossible to probe with alpha-helices embedded in folded proteins. Here, we use designed peptides to examine the effect of strand length on antiparallel beta-sheet stability. alpha-Helices become more stable as they grow longer. Our data show that a two-stranded beta-sheet ("beta-hairpin") becomes more stable when the strands are lengthened from five to seven residues, but that further strand lengthening to nine residues does not lead to further beta-hairpin stabiliza

SUBMITTER: Stanger HE 

PROVIDER: S-EPMC59824 | biostudies-literature | 2001 Oct

REPOSITORIES: biostudies-literature