{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,9]],"date-time":"2026-04-09T22:35:49Z","timestamp":1775774149278,"version":"3.50.1"},"reference-count":22,"publisher":"Oxford University Press (OUP)","issue":"12","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2006,6,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>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.<\/jats:p>\n               <jats:p>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\u2013sidechain hydrogen bonding from 181 in our previous analysis to 202 in this analysis.<\/jats:p>\n               <jats:p>Availability: \u00a0<\/jats:p>\n               <jats:p>Contact: \u00a0andrew@bioinf.org.uk<\/jats:p>","DOI":"10.1093\/bioinformatics\/btl120","type":"journal-article","created":{"date-parts":[[2006,4,7]],"date-time":"2006-04-07T00:24:36Z","timestamp":1144369476000},"page":"1464-1470","source":"Crossref","is-referenced-by-count":17,"title":["Analysing the ability to retain sidechain hydrogen-bonds in mutant proteins"],"prefix":"10.1093","volume":"22","author":[{"given":"Alison L.","family":"Cuff","sequence":"first","affiliation":[{"name":"School of Animal and Microbial Sciences, University of Reading 1 \u00a0 1 \u00a0 \u00a0 Whiteknights, PO Box 228, Reading RG6 6AJ, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert W.","family":"Janes","sequence":"additional","affiliation":[{"name":"School of Biological and Chemical Sciences, Queen Mary, University of London 2 \u00a0 2 \u00a0 \u00a0 Mile End Road, London E1 4NS, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrew C.R.","family":"Martin","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University College London 3 \u00a0 3 \u00a0 \u00a0 Gower Street, London WC1E 6BT, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2006,4,6]]},"reference":[{"key":"2023012408414163700_b1","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1038\/330041a0","article-title":"Contributions of hydrogen bonds of Thr157 to the thermodynamic stability of phage T4 lysozyme","volume":"330","author":"Alber","year":"1987","journal-title":"Nature (London)"},{"key":"2023012408414163700_b2","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/0079-6107(84)90007-5","article-title":"Hydrogen bonding in globular proteins","volume":"44","author":"Baker","year":"1984","journal-title":"Progr. 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