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Analysing the ability to retain sidechain hydrogen-bonds in mutant proteins

Cuff, A. L., Janes, R. W. and Martin, A. C. R. (2006) Analysing the ability to retain sidechain hydrogen-bonds in mutant proteins. Bioinformatics, 22 (12). pp. 1464-1470. ISSN 1367-4803

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To link to this item DOI: 10.1093/bioinformatics/btl120

Abstract/Summary

Motivation: Hydrogen bonds are one of the most important inter-atomic interactions in biology. Previous experimental, theoretical and bioinformatics analyses have shown that the hydrogen bonding potential of amino acids is generally satisfied and that buried unsatisfied hydrogen-bond-capable residues are destabilizing. When studying mutant proteins, or introducing mutations to residues involved in hydrogen bonding, one needs to know whether a hydrogen bond can be maintained. Our aim, therefore, was to develop a rapid method to evaluate whether a sidechain can form a hydrogen-bond. Results: A novel knowledge-based approach was developed in which the conformations accessible to the residues involved are taken into account. Residues involved in hydrogen bonds in a set of high resolution crystal structures were analyzed and this analysis is then applied to a given protein. The program was applied to assess mutations in the tumour-suppressor protein, p53. This raised the number of distinct mutations identified as disrupting sidechain-sidechain hydrogen bonding from 181 in our previous analysis to 202 in this analysis.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences
ID Code:10142
Uncontrolled Keywords:SECONDARY STRUCTURE FORMATION, FREE-ENERGY DETERMINANTS, GLOBULAR-PROTEINS, STABILITY, DYNAMICS, TUMOR

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