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

摘要: Apparent electrostatics-defying clustering of arginines attributed as screening effect solvent is in this study examined a possible thermodynamic driving force protein–protein interaction. A dataset 266 protein dimers found to have ∼22% mutually paired and ∼17% pairs interaction across interfaces thus putative “hotspots” The pairing, uncorrelated with inter or intramolecular context, could be contributing folding well, and, access, driven by effects that are generic structures. Mutually stacked at shorter distances but diverse geometrical modes otherwise, the cations tend gross deficit hydrogen-bond partners, electrostatics interface that, on average, repulsive for Embedded local environment enriched polarizable residues, aromatic, aliphatic, anionic, may contribute via environmental polarization response cation clustering, new principle molecular recognition. Proteins 2009. © 2008 Wiley-Liss, Inc.