Parallel β-Sheet Secondary Structure Is Stabilized and Terminated by Interstrand Disulfide Cross-Linking

被引：57

作者：

Almeida, Aaron M. ^{[1
]}

Li, Rebecca ^{[1
]}

Gellman, Samuel H. ^{[1
]}

机构：

[1] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2012年 / 134卷 / 01期

基金：

美国国家科学基金会;

关键词：

ALPHA-HELICAL CONFORMATION; RING-CLOSING METATHESIS; HYDROGEN-BOND SURROGATE; SIDE-CHAIN INTERACTIONS; GLOBULAR-PROTEINS; HAIRPIN PEPTIDES; TURN MIMETICS; MODEL SYSTEMS; AMINO-ACIDS; DESIGN;

D O I：

10.1021/ja208856c

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Disulfide bonds between Cys residues in adjacent strands of parallel beta-sheets are rare among proteins, which suggests that parallel beta-sheet structure is not stabilized by such disulfide cross-links. We report experimental results that show, surprisingly, that an interstrand disulfide bond can stabilize parallel beta-sheets formed by an autonomously folding peptide in aqueous solution. NMR analysis reveals that parallel beta-sheet structure is terminated beyond the disulfide bond, which causes deviation from the extended backbone conformation at one of the Cys residues.

引用

页码：75 / 78

页数：4

共 68 条

[1]

BALARAM H, 1990, INT J PEPT PROT RES, V35, P495

[2] ALPHA-HELIX FORMATION BY PEPTIDES OF DEFINED SEQUENCE [J].