ProtorP: a protein–protein interaction analysis server

The PROTORP server analyses protein–protein associations in 3D structures. The server calculates a series of physical and chemical parameters of the protein interaction sites that contribute to the binding energy of the association. These parameters include, size and shape, intermolecular bonding, r...

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Bibliographic Details
Published inBioinformatics Vol. 25; no. 3; pp. 413 - 414
Main Authors Reynolds, Christopher, Damerell, David, Jones, Susan
Format Journal Article
LanguageEnglish
Published Oxford Oxford University Press 01.02.2009
Oxford Publishing Limited (England)
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Summary:The PROTORP server analyses protein–protein associations in 3D structures. The server calculates a series of physical and chemical parameters of the protein interaction sites that contribute to the binding energy of the association. These parameters include, size and shape, intermolecular bonding, residue and atom composition and secondary structure contributions. The server is flexible, in that it allows users to analyse individual protein associations or large datasets of associations deposited in the PDB, or upload and analyse proprietary files. The properties calculated can be compared with parameter distributions for non-homologous datasets of different classes of protein associations provided on the server website. The server provides an efficient way of characterizing protein–protein associations of new or existing proteins, and a means of putting these values in the context of previously observed associations. Availability: http://www.bioinformatics.sussex.ac.uk/protorp Contact: s.jones@sussex.ac.uk
Bibliography:ark:/67375/HXZ-NHVVSL0W-4
To whom correspondence should be addressed.
istex:075AADF573B268388DC060A0E2A205690A78D1B1
Associate Editor: Burkhard Rost
ArticleID:btn584
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1367-4803
1460-2059
1367-4811
DOI:10.1093/bioinformatics/btn584