Formation and stability of β-hairpin structures in polypeptides

被引：148

作者：

Blanco, F ^{[1
]}

Ramírez-Alvarado, M ^{[1
]}

Serrano, L ^{[1
]}

机构：

[1] European Mol Biol Lab, D-69117 Heidelberg, Germany

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1998年 / 8卷 / 01期

关键词：

D O I：

10.1016/S0959-440X(98)80017-1

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：

Experimental work on peptide models with beta-hairpin structures has provided new insights into the formation and stability of this secondary structure element. Both the turn region and the antiparallel strand residues not only affect the overall stability of the hairpin, but also determine the type of hairpin formed. These results agree reasonably well with those from experimental and statistical analyses of beta-sheet structures in proteins.

引用

页码：107 / 111

页数：5

共 28 条

[1] NMR EVIDENCE OF A SHORT LINEAR PEPTIDE THAT FOLDS INTO A BETA-HAIRPIN IN AQUEOUS-SOLUTION [J].