Electrostatic aspects of protein-protein interactions.
Structural and mutational analyses reveal a central role for electrostatic interactions in protein-protein association. Experiment and theory both demonstrate that clusters of charged and polar residues that are located on protein-protein interfaces may enhance complex stability, although the total effect of electrostatics is generally net destabilizing. The past year also witnessed significant progress in our understanding of the effect of electrostatics on protein association kinetics, specifically in the characterization of a partially desolvated encounter complex.
Sheinerman
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FB
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. fbs5@columbia.edu
Norel
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Honig
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B
D000818:Animals; D019295:Computational Biology; D004058:Diffusion; D006801:Humans; D006860:Hydrogen Bonding; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D055672:Static Electricity; D013499:Surface Properties; D013816:Thermodynamics
D011506:Proteins