@article{(Open Science Index):https://publications.waset.org/pdf/5196,
	  title     = {Identification and Analysis of Binding Site Residues in Protein-Protein Complexes},
	  author    = {M. Michael Gromiha and  Kiyonobu Yokota and  Kazuhiko Fukui},
	  country	= {},
	  institution	= {},
	  abstract     = {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.
},
	    journal   = {International Journal of Bioengineering and Life Sciences},
	  volume    = {3},
	  number    = {9},
	  year      = {2009},
	  pages     = {415 - 420},
	  ee        = {https://publications.waset.org/pdf/5196},
	  url   	= {https://publications.waset.org/vol/33},
	  bibsource = {https://publications.waset.org/},
	  issn  	= {eISSN: 1307-6892},
	  publisher = {World Academy of Science, Engineering and Technology},
	  index 	= {Open Science Index 33, 2009},
	}