Document Type
Article
Publication Date
6-2011
Publication Title
Physical Biology
Volume
8
Issue
3
Publisher
IOP Publishing
Abstract
The role of electrostatics in protein–protein interactions and binding is reviewed in this paper. A brief outline of the computational modeling, in the framework of continuum electrostatics, is presented and the basic electrostatic effects occurring upon the formation of the complex are discussed. The effect of the salt concentration and pH of the water phase on protein–protein binding free energy is demonstrated which indicates that the increase of the salt concentration tends to weaken the binding, an observation that is attributed to the optimization of the charge–charge interactions across the interface. It is pointed out that the pH-optimum (pH of optimal binding affinity) varies among the protein–protein complexes, and perhaps is a result of their adaptation to particular subcellular compartments. The similarities and differences between hetero- and homo-complexes are outlined and discussed with respect to the binding mode and charge complementarity.
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Comments
This manuscript has been published in the journal Physical Biology. Please find the published version here (note that a subscription is necessary to access this version):
http://iopscience.iop.org/1478-3975/8/3/035001/fulltext/