%0 Journal Article
	%A M. Michael Gromiha and  Kiyonobu Yokota and  Kazuhiko Fukui
	%D 2009
	%J International Journal of Bioengineering and Life Sciences
	%B World Academy of Science, Engineering and Technology
	%I Open Science Index 33, 2009
	%T Identification and Analysis of Binding Site Residues in Protein-Protein Complexes
	%U https://publications.waset.org/pdf/5196
	%V 33
	%X We have developed an energy based approach for identifying the binding sites and important residues for binding in protein-protein complexes. We found that the residues and residuepairs with charged and aromatic side chains are important for binding. These residues influence to form cation-¤Ç, electrostatic and aromatic interactions. Our observation has been verified with the experimental binding specificity of protein-protein complexes and found good agreement with experiments. The analysis on surrounding hydrophobicity reveals that the binding residues are less hydrophobic than non-binding sites, which suggests that the hydrophobic core are important for folding and stability whereas the surface seeking residues play a critical role in binding. Further, the propensity of residues in the binding sites of receptors and ligands, number of medium and long-range contacts, and influence of neighboring residues will be discussed.

	%P 415 - 420