Protein protein recognition is an important step in biological processes, which still largely remains elusive. The inter residue contact potential, CP ij , describes the propensity of contact between two type...Protein protein recognition is an important step in biological processes, which still largely remains elusive. The inter residue contact potential, CP ij , describes the propensity of contact between two types of residue. In this study, several different CP ij variants were examined with the objective of discriminating the binding potential of surface pairs. Using solvent mediated inter molecule contact potential (SM IMCP ij ), an evaluation model was deduced and tested. Using the evaluation model it was found that the SM IMCP ij gives a better performance than either residue mediated IMCP ij (RM IMCP ij ) or folding residue contact potential (FCP ij ). The results suggest that the evaluation model provides a fast, effective, and discriminative method for the evaluation of proposed binding interfaces.展开更多
基金Supported by the National Natural Science Foundation (No.39970 15 5 ) the High- Technology Developm entProgram of China (No.2 0 0 1AA 2 330 11) +1 种基金and theNational Frontier Research Program (No.G19990 75 6 0 2 G19990 1190 2 and19980 5 110 5 )
文摘Protein protein recognition is an important step in biological processes, which still largely remains elusive. The inter residue contact potential, CP ij , describes the propensity of contact between two types of residue. In this study, several different CP ij variants were examined with the objective of discriminating the binding potential of surface pairs. Using solvent mediated inter molecule contact potential (SM IMCP ij ), an evaluation model was deduced and tested. Using the evaluation model it was found that the SM IMCP ij gives a better performance than either residue mediated IMCP ij (RM IMCP ij ) or folding residue contact potential (FCP ij ). The results suggest that the evaluation model provides a fast, effective, and discriminative method for the evaluation of proposed binding interfaces.
