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dc.contributor.authorHuang, Bingding
dc.contributor.authorSchroeder, Michael
dc.contributor.editorTorda, Andrew
dc.contributor.editorKurtz, Stefan
dc.contributor.editorRarey, Matthias
dc.date.accessioned2019-08-27T08:22:36Z
dc.date.available2019-08-27T08:22:36Z
dc.date.issued2005
dc.identifier.isbn3-88579-400-4
dc.identifier.issn1617-5468
dc.identifier.urihttp://dl.gi.de/handle/20.500.12116/24930
dc.description.abstractProtein-protein interactions are fundamental as many proteins mediate their biological function through protein interactions. Over the past 20 years there have been many computational approaches to dock proteins. These approaches are mostly based on the shape complementarity of structures and the physio-chemical properties of the interfaces. However, these docking approaches are far from perfect and there still remains potential space to improve. We propose to use family-based residue interaction propensity as well as the tightness of fit between residues with high propensities as a scoring function to improve rigid body docking. This approach is evaluated on an established benchmark data set. Our scoring function improves the number of hits for enzyme-inhibitor complexes by a factor of 4-30 in comparison with shape complementarity alone and for antibodyantigen complexes by 4-11. The supplementary data are available at http://www.biotec.tu-dresden. de/\~bhuang/bdock.en
dc.language.isoen
dc.publisherGesellschaft für Informatik e.V.
dc.relation.ispartofGerman Conference on Bioinformatics 2005 (GCB 2005)
dc.relation.ispartofseriesLecture Notes in Informatics (LNI) - Proceedings, Volume P-71
dc.titleUsing residue propensities and tightness of fit to improve rigid-body protein-protein dockingen
dc.typeText/Conference Paper
dc.pubPlaceBonn
mci.reference.pages159-173
mci.conference.sessiontitleRegular Research Papers
mci.conference.locationHamburg
mci.conference.date5.-7. Oktober 2005


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