Exploiting residue-level and profile-level interface propensities for usage in binding sites prediction of proteins.

ABSTRACT:

Background

Recognition of binding sites in proteins is a direct computational approach to the characterization of proteins in terms of biological and biochemical function. Residue preferences have been widely used in many studies but the results are often not satisfactory. Although different amino acid compositions among the interaction sites of different complexes have been observed, such differences have not been integrated into the prediction process. Furthermore, the evolution information has not been exploited to achieve a more powerful propensity.

Result

In this study, the residue interface propensities of four kinds of complexes (homo-permanent complexes, homo-transient complexes, hetero-permanent complexes and hetero-transient complexes) are investigated. These prope

SUBMITTER: Dong Q 

PROVIDER: S-EPMC1885810 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature