How do crystal lattice contacts reveal protein crystallization mechanism?

被引：14

作者：

Nanev, Christo N. ^{[1
]}

机构：

[1] Bulgarian Acad Sci, Rostislaw Kaischew Inst Phys Chem, BU-1113 Sofia, Bulgaria

来源：

CRYSTAL RESEARCH AND TECHNOLOGY | 2008年 / 43卷 / 09期

关键词：

protein crystal lattice contacts; L-arginine and L-glutamine; L-lysine; L-glutamic acid; protein crystal nucleation;

D O I：

10.1002/crat.200800214

中图分类号：

O7 [晶体学];

学科分类号：

0702 ; 070205 ; 0703 ; 080501 ;

摘要：

The nature of crystal lattice contacts is discussed because they reflect the selection of the most appropriate (for the given set of conditions) contact patches on the surface of protein molecules. The conclusion is that, along with chemical composition, the protein structure at the crystal lattice contacts is the key to crystallization behavior. The reason is that most stable are conformations, which do not only maximize the number of the bonds but simultaneously minimize van der Waals repulsions. A plausible explanation of the crystallization slot that exists for proteins is given on this basis. (C) 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：914 / 920

页数：7

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