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Electrostatics-defying interaction between arginine termini as a thermodynamic driving force in protein-protein interaction

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Title Electrostatics-defying interaction between arginine termini as a thermodynamic driving force in protein-protein interaction
 
Creator PEDNEKAR, D
TENDULKAR, A
DURANI, S
 
Subject cation-pi interactions
guanidinium ion-pair
acid side-chains
mean force
molecular simulation
recognition sites
residues
water
interfaces
systems
protein-protein interaction
hotspots
arginine-arginine interaction
cation-pi bond
molecular recognition
polarization effect
 
Description Apparent electrostatics-defying clustering of arginines attributed as screening effect of solvent is in this study examined as a possible thermodynamic driving force in protein-protein interaction. A dataset of 266 protein dimers is found to have similar to 22% arginines mutually paired and similar to 17% pairs in interaction across interfaces and thus putative "hotspots" of protein-protein interaction. The pairing, uncorrelated with inter or intramolecular context, could be contributing in protein folding as well, and, uncorrelated with solvent access, could be driven by effects that are generic to solvent and protein structures. Mutually stacked at shorter distances but in diverse geometrical modes otherwise, the cations tend to be in gross deficit of hydrogen-bond partners, and contributing electrostatics across protein-protein interface that, on average, is repulsive for protein-protein interaction. Embedded in local environment enriched in polarizable residues, aromatic, aliphatic, and anionic, the arginines may contribute to protein-protein interaction via environmental polarization response to electrostatics of cation clustering, a possible new principle in molecular recognition.
 
Publisher WILEY-LISS
 
Date 2011-09-01T13:16:55Z
2011-12-26T12:59:40Z
2011-12-27T05:52:16Z
2011-09-01T13:16:55Z
2011-12-26T12:59:40Z
2011-12-27T05:52:16Z
2009
 
Type Article
 
Identifier PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 74(1), 155-163
0887-3585
http://dx.doi.org/10.1002/prot.22142
http://dspace.library.iitb.ac.in/xmlui/handle/10054/12787
http://hdl.handle.net/10054/12787
 
Language en