Do interstrand hydrogen bonds contribute to β-hairpin peptide stability in solution?: IR analysis of peptide folding in water

被引：22

作者：

Colley, CS ^{[1
]}

Griffiths-Jones, SR ^{[1
]}

George, MW ^{[1
]}

Searle, MS ^{[1
]}

机构：

[1] Univ Nottingham, Dept Chem, Nottingham NG7 2RD, England

来源：

CHEMICAL COMMUNICATIONS | 2000年 / 07期

关键词：

D O I：

10.1039/b000426j

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The amide I carbonyl stretch in the IR spectrum, together with H-1 NMR H alpha chemical shifts, have been used to investigate the folding of a 16-residue beta-hairpin peptide in water: while H alpha shifts are consistent with a significant population of the folded state (ca. 40%), we see no features in the IR spectrum in the amide I region to suggest a significant contribution from interstrand hydrogen bonds, although at high peptide concentration (greater than or equal to 10 mM) the appearance of a new band at 1616 cm(-1) is consistent with the onset of irreversible peptide aggregation.

引用

页码：593 / 594

页数：2

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