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ABSTRACT: Background
Protein binding site prediction by computational means can yield valuable information that complements and guides experimental approaches to determine the structure of protein complexes. Predictions become even more relevant and timely given the current resolution of protein interaction maps, where there is a very large and still expanding gap between the available information on: (i) which proteins interact and (ii) how proteins interact. Proteins interact through exposed residues that present differential physicochemical properties, and these can be exploited to identify protein interfaces.Results
Here we present VORFFIP, a novel method for protein binding site prediction. The method makes use of broad set of heterogeneous data and defined of residue environmen
SUBMITTER: Segura J
PROVIDER: S-EPMC3171731 | biostudies-literature | 2011 Aug
REPOSITORIES: biostudies-literature