Electrostatics-defying interaction between arginine termini as a thermodynamic driving force in protein-protein interaction
DSpace at IIT Bombay
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Title |
Electrostatics-defying interaction between arginine termini as a thermodynamic driving force in protein-protein interaction
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Creator |
PEDNEKAR, D
TENDULKAR, A DURANI, S |
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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 |
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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.
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Publisher |
WILEY-LISS
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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 |
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Type |
Article
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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 |
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Language |
en
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