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Analysis of protein-protein interaction sites using surface patches.

Jones, S; Thornton, JM; (1997) Analysis of protein-protein interaction sites using surface patches. J Mol Biol , 272 (1) 121 - 132. 10.1006/jmbi.1997.1234.

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Protein-protein interaction sites in complexes of known structure are characterised using a series of parameters to evaluate what differentiates them from other sites on the protein surface. Surface patches are defined in protomers from a data set of 28 homo-dimers, 20 different hetero-complexes (segregated into large and small protomers), and antigens from six antibody-antigen complexes. Six parameters (solvation potential, residue interface propensity, hydrophobicity, planarity, protrusion and accessible surface area) are calculated for the observed interface patch and all other surface patches defined on each protein. A ranking of the observed interface, relative to all other possible patches, is calculated. With this approach it becomes possible to analyse the distribution of the rankings of all the observed patches, relative to all other surface patches, for each data set. For each type of complex, none of the parameters were definitive, but the majority showed trends for the observed interface to be distinguished from other surface patches.

Type: Article
Title: Analysis of protein-protein interaction sites using surface patches.
Location: ENGLAND
DOI: 10.1006/jmbi.1997.1234
Language: English
Keywords: Animals, Antigens, Binding Sites, Dimerization, Humans, Models, Chemical, Protein Binding, Proteins, Surface Properties
UCL classification: UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)
URI: http://discovery.ucl.ac.uk/id/eprint/21715
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