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.
%0 Journal Article
%1 Shei_2000_153
%A Sheinerman, F. B.
%A Norel, R.
%A Honig, B.
%D 2000
%J Curr. Opin. Struct. Biol.
%K Animals; Binding; Biology; Bonding; Computational Conformation; Diffusion; Electrostatics; Humans; Hydrogen Kinetics; Mutagenesis, Properties; Protein Proteins, Site-Directed; Structure, Surface Tertiary; Thermodynamics chemistry/metabolism;
%N 2
%P 153--159
%T Electrostatic aspects of protein-protein interactions.
%V 10
%X 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.
@article{Shei_2000_153,
abstract = {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.},
added-at = {2009-06-03T11:20:58.000+0200},
author = {Sheinerman, F. B. and Norel, R. and Honig, B.},
biburl = {https://www.bibsonomy.org/bibtex/25f514f67ffa8af117d03b5f55a5acfc8/hake},
description = {The whole bibliography file I use.},
file = {Shei_2000_153.pdf:Shei_2000_153.pdf:PDF},
institution = {Department of Biochemistry and Molecular Biophysics, Columbia University,
New York, NY 10032, USA. fbs5@columbia.edu},
interhash = {2071acd3199120cc21e25578273a2f92},
intrahash = {5f514f67ffa8af117d03b5f55a5acfc8},
journal = {Curr. Opin. Struct. Biol.},
keywords = {Animals; Binding; Biology; Bonding; Computational Conformation; Diffusion; Electrostatics; Humans; Hydrogen Kinetics; Mutagenesis, Properties; Protein Proteins, Site-Directed; Structure, Surface Tertiary; Thermodynamics chemistry/metabolism;},
month = Apr,
number = 2,
pages = {153--159},
pdf = {Shei_2000_153.pdf},
pii = {S0959-440X(00)00065-8},
pmid = {10753808},
timestamp = {2009-06-03T11:21:30.000+0200},
title = {Electrostatic aspects of protein-protein interactions.},
volume = 10,
year = 2000
}