Unusual β-sheet periodicity in small cyclic peptides

被引：109

作者：

Gibbs, AC

Kondejewski, LH

Gronwald, W

Nip, AM

Hodges, RS

Sykes, BD

Wishart, DS ^{[1
]}

机构：

[1] Univ Alberta, Fac Pharm & Pharmaceut Sci, Edmonton, AB T6G 2N8, Canada

[2] Univ Alberta, Prot Engn Network Ctr Excellence, Edmonton, AB T6G 2N8, Canada

[3] Univ Alberta, Dept Biochem, Edmonton, AB T6G 2N8, Canada

来源：

NATURE STRUCTURAL BIOLOGY | 1998年 / 5卷 / 04期

关键词：

D O I：

10.1038/nsb0498-284

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cyclic peptide homologs of gramicidin S containing 6, 8, 10, 12, 14 and 16 residues were synthesized and characterized using circular dichroism (CD) and (1)H 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.

引用

页码：284 / 288

页数：5

共 35 条

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[2]

[Anonymous], 1986, NMR of Proteins and Nucleic Acids

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