Browse by author
Lookup NU author(s): Dr Simon CockellORCiD
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Motivation: Due to the limitations in experimental methods for determining binary interactions and structure determination of protein complexes, the need exists for computational models to fill the increasing gap between genome sequence information and protein annotation. Here we describe a novel method that uses structural models to reduce a large number of in silico predictions to a high confidence subset that is amenable to experimental validation. Results: A two-stage evaluation procedure was developed, first, a sequence-based method assessed the conservation of protein interface patches used in the original in silico prediction method, both in terms of position within the primary sequence, and in terms of sequence conservation. When applying the most stringent conditions it was found that 20.5% of the data set being assessed passed this test. Secondly, a high-throughput structure-based docking evaluation procedure assessed the soundness of three dimensional models produced for the putative interactions. Of the data set being assessed, 8264 interactions or over 70% could be modelled in this way, and 27% of these can be considered ‘valid’ by the applied criteria. In all, 6.9% of the interactions passed both the tests and can be considered to be a high confidence set of predicted interactions, several of which are described.
Author(s): Cockell SJ, Baldo O, Jackson RM
Publication type: Article
Publication status: Published
Journal: Bioinformatics
Year: 2007
Volume: 23
Issue: 5
Pages: 573-581
ISSN (print): 1367-4803
ISSN (electronic): 1367-4811
Publisher: Oxford University Press
URL: http://dx.doi.org/10.1093/bioinformatics/btl661
DOI: 10.1093/bioinformatics/btl661
Altmetrics provided by Altmetric
