Comparison Of Residues Conformation Optimized Degree Between Protein-protein Interface And Non-interface Surface

A data set of 55 non-homologue complexes containing both bound and unbound proteins are studied to illustrate the difference of optimizing degrees of local backbone and side chain residual conformations between on protein-protein interface and on non-interface surface, the change of optimizing degrees of local backbone and side chain residual conformations of both interface residues and non-interface surface residues when the monomers associate to a complex and the difference of the changing trends when associating . The following texts are our findings:Optimizing degrees of local backbone and side chain residual conformations have been quantified.According to the result of'the differences of optimizing degrees of residual types distribution modeled on local backbone conformation between protein-protein interface and non-interface surface'and'the differences of optimizing degrees of local backbone conformation concerning to residual type distribution between protein-protein interface and non-interface surface', a conclusion can be draw that protein-protein interface residual local backbone conformation optimizing degrees are lower than non-interface surface.An important character of protein-protein interface residues have found: residual side-chain conformation modeled on defined local backbone optimizing degree is lower than non-interface surface.Some tubby types of residues whose side-chain are short occur great changes on side-chain conformation and their optimizing degrees decrease when proteins change from unbound to bound. These residues have high side-chain conformation optimizing degree and do not belong to the lowest 5% in the rank of optimizing degrees in unbound. Some slight types of residue whose side-chain are long occur great changes on...