Extent of hydrogen-bond protection in folded proteins:: A constraint on packing architectures

被引：42

作者：

Fernández, A

Berry, RS

机构：

[1] Univ Chicago, Inst Biophys Dynam, Chicago, IL 60637 USA

[2] Univ Nacl Sur, Consejo Nacl Invest Cient & Tecn, Inst Matemat, RA-8000 Bahia Blanca, Buenos Aires, Argentina

[3] Univ Chicago, James Franck Inst, Chicago, IL 60637 USA

[4] Univ Chicago, Dept Chem, Chicago, IL 60637 USA

来源：

BIOPHYSICAL JOURNAL | 2002年 / 83卷 / 05期

关键词：

D O I：

10.1016/S0006-3495(02)75258-2

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Progressive structuring and ultimately exclusion of water by hydrophobes surrounding backbone hydrogen bonds turn the latter into guiding factors of protein folding. Here we demonstrate that an arrangement of five hydrophobes yields an optimal hydrogen-bond stabilization. This motif is shown to be nearly ubiquitous in native folds.

引用

页码：2475 / 2481

页数：7

共 19 条

[1] Inter-residue potentials in globular proteins and the dominance of highly specific hydrophilic interactions at close separation [J].