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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*
1
Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California
2
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