Computation of electrostatic complements to proteins: A case of charge stabilized binding

被引：66

作者：

Chong, LT ^{[1
]}

Dempster, SE ^{[1
]}

Hendsch, ZS ^{[1
]}

Lee, LP ^{[1
]}

Tidor, B ^{[1
]}

机构：

[1] MIT, Dept Chem, Cambridge, MA 02139 USA

来源：

PROTEIN SCIENCE | 1998年 / 7卷 / 01期

关键词：

continuum electrostatics; electrostatic complement; protein binding; rational ligand design;

D O I：

10.1002/pro.5560070122

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：

Recent evidence suggests that the net effect of electrostatics is generally to destabilize protein binding due to large desolvation penalties. A novel method for computing ligand-charge distributions that optimize the tradeoff between ligand desolvation penalty and favorable interactions with a binding site has been applied to a model for barnase. The result is a ligand-charge distribution with a favorable electrostatic contribution to binding due, in part, to ligand point charges whose direct interaction with the binding site is unfavorable, but which make strong intra-molecular interactions that are uncloaked on binding and thus act to lessen the ligand desolvation penalty.

引用

页码：206 / 210

页数：5

共 30 条

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