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Optimal Docking Area: A New Method for Predicting ProteinProtein Interaction Sites

Summary: Optimal Docking Area: A New Method for Predicting
Protein­Protein Interaction Sites
Juan Fernandez-Recio,1
Max Totrov,2
Constantin Skorodumov,2
and Ruben Abagyan1*
Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California
Molsoft, LLC, 3366 Torrey Pines Court, La Jolla, California
ABSTRACT Understanding energetics and
mechanism of protein­protein association remains
one of the biggest theoretical problems in structural
biology. It is assumed that desolvation must play an
essential role during the association process, and
indeed protein­protein interfaces in obligate com-
plexes have been found to be highly hydrophobic.
However, the identification of protein interaction
sites from surface analysis of proteins involved in
non-obligate protein­protein complexes is more


Source: Abagyan, Ruben - School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego


Collections: Biology and Medicine