@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}, }