GUIDELINES FOR PROTEIN DESIGN - THE ENERGETICS OF BETA-SHEET SIDE-CHAIN INTERACTIONS

被引：237

作者：

SMITH, CK ^{[1
]}

REGAN, L ^{[1
]}

机构：

[1] YALE UNIV, DEPT MOLEC BIOPHYS & BIOCHEM, NEW HAVEN, CT 06520 USA

来源：

SCIENCE | 1995年 / 270卷 / 5238期

关键词：

D O I：

10.1126/science.270.5238.980

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

To determine the interaction energy between cross-strand pairs of side chains on an antiparallel beta sheet, pairwise amino acid substitutions were made on the solvent-exposed face of the B1 domain of streptococcal protein G, The measured interaction energies were substantial (1.8 kilocalories per mole) and comparable to the magnitude of the beta sheet propensities. The experimental results paralleled the statistical frequency with which the residue pairs are found in beta sheets of known structure.

引用

页码：980 / 982

页数：3

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