| Literature DB >> 9546219 |
A C Gibbs1, L H Kondejewski, W Gronwald, A M Nip, R S Hodges, B D Sykes, D S Wishart.
Abstract
Cyclic peptide homologs of gramicidin S containing 6, 8, 10, 12, 14 and 16 residues were synthesized and characterized using circular dichroism (CD) and 1H NMR spectroscopy. Based on the three-dimensional structures generated from these data we have found strong evidence of a periodic sequence-length dependence on beta-sheet content. In particular, peptides of length 6, 10 and 14 residues exhibit a high beta-sheet content, while peptides of 8, 12 and 16 residues appear to exist as random coils. This unusual beta-sheet periodicity may have important implications in our understanding of beta-sheet formation and in the design of constrained beta-sheet and beta-hairpin mimics.Entities:
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Year: 1998 PMID: 9546219 DOI: 10.1038/nsb0498-284
Source DB: PubMed Journal: Nat Struct Biol ISSN: 1072-8368