How the excluded volume architecture influences ion-mediated forces between proteins

被引：10

作者：

Dahirel, V. ^{[1
]}

Jardat, M. ^{[1
]}

Dufreche, J. -F. ^{[1
]}

Turq, P. ^{[1
]}

机构：

[1] Univ Paris 06, CNRS, Lab Liquides Ion & Interfaces Chargees, UMR 7612, F-75252 Paris 05, France

来源：

PHYSICAL REVIEW E | 2007年 / 76卷 / 04期

关键词：

D O I：

10.1103/PhysRevE.76.040902

中图分类号：

O35 [流体力学]; O53 [等离子体物理学];

学科分类号：

070204 ; 080103 ; 080704 ;

摘要：

The effective interactions between model proteins of various shapes are computed by means of Monte Carlo simulations. In particular, we determine how the modification of the excluded volume architecture influences both entropic and purely electrostatic ion-mediated forces between proteins. We find that interprotein interactions are strongly affected by protein shape, which results in a high decrease of electrostatic screening for typical active site geometries. Effective interactions are then closer to the direct Coulombic interactions, and both affinity and selectivity are enhanced by several orders of magnitude.

引用

页数：4

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