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Data‐driven models for protein interaction and design
Author(s) -
Zhu Xiaolei,
Ericksen Spencer S.,
Demerdash Omar N. A.,
Mitchell Julie C.
Publication year - 2013
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24405
Subject(s) - interface (matter) , computational biology , protein–protein interaction , computer science , hemagglutinin (influenza) , point mutation , high resolution , plasma protein binding , binding site , human–computer interaction , chemistry , biology , mutation , genetics , biochemistry , geography , gene , gibbs isotherm , remote sensing , pulmonary surfactant
We describe methods and results for four new types of challenge in the Critical Assessment of PRedicted Interactions (CAPRI). Two new challenges asked predictors to create models related to protein interface design. The first of these was to distinguish binding interfaces from designed nonbinding interfaces. The second was to predict the effects of all single‐point mutations on hemagglutinin binding to two small designed proteins. Two additional challenges asked predictors to submit high‐resolution structures for interface‐bound crystallographic waters and for binding heparin to a putative glycosylase. Proteins 2013; 81:2221–2228. © 2013 Wiley Periodicals, Inc.