MOLECULAR-INTERACTIONS IN PROTEIN CRYSTALS - SOLVENT ACCESSIBLE SURFACE AND STABILITY

被引：44

作者：

ISLAM, SA

WEAVER, DL

机构：

[1] TUFTS UNIV,DEPT PHYS,MEDFORD,MA 02155

[2] IMPERIAL CANC RES FUND,BIOMOLEC MODELLING LAB,LONDON WC2A 3PX,ENGLAND

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1990年 / 8卷 / 01期

关键词：

accessible area; crystalline environment; dimeric proteins; hydrophobic interaction; linear correlation; monomeric proteins;

D O I：

10.1002/prot.340080103

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：

The accessible surface areas of 58 monomeric and dimeric proteins, when measured in the crystalline environment, are found to be simply related to molecular weight. The loss of accessible surface when the proteins go from a free to their crystalline environment is well defined, implying that the hydrophobic interaction, which has been found to contribute to protein folding and stability in living systems, also contributes to protein crystal stability. Copyright © 1990 Wiley‐Liss, Inc.

引用

页码：1 / 5

页数：5

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