Comparative structures and properties of elastic proteins

被引：66

作者：

Tatham, AS ^{[1
]}

Shewry, PR ^{[1
]}

机构：

[1] Univ Bristol, Dept Agr Sci, Long Ashton Res Stn, Inst Arable Crops Res, Bristol BS41 9AF, Avon, England

来源：

PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES | 2002年 / 357卷 / 1418期

关键词：

elasticity; repeat motif; rubber;

D O I：

10.1098/rstb.2001.1031

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Elastic proteins are characterized by being able to undergo significant deformation, without rupture, before returning to their original state when the stress is removed. The sequences of elastic proteins contain elastomeric domains, which comprise repeated sequences, which in many cases appear to form P-turns. In addition, the majority also contain domains that form intermolecular cross-links, which may be covalent or non-covalent. The mechanism of elasticity varies between the different proteins and appears to be related to the biological role of the protein.

引用

页码：229 / 234

页数：6

共 47 条

[41] ENTROPIC ELASTIC PROCESSES IN PROTEIN MECHANISMS .1. ELASTIC STRUCTURE DUE TO AN INVERSE TEMPERATURE TRANSITION AND ELASTICITY DUE TO INTERNAL CHAIN DYNAMICS [J].