{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T11:50:44Z","timestamp":1792065044728,"version":"4.4.0"},"reference-count":30,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T00:00:00Z","timestamp":1789776000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T00:00:00Z","timestamp":1789776000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Peptide Science"],"published-print":{"date-parts":[[2026,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>Hydrogen bonds contribute substantially to the stabilisation of specific three\u2010dimensional structures of peptides. The C5 hydrogen bond is an intraresidue interaction, which appears to contribute to the stabilisation of fully extended residue conformations, with backbone torsion angles (\u03c6, \u03c8) lying close to \u00b1180\u00b0. The present study revisits the occurrence of C5 conformations in proteins, using a high\u2010resolution, non\u2010homologous dataset of 6924 x\u2010ray diffraction structures (sequence identity &lt;\u200930%, resolution &lt;\u20091.6\u2009\u00c5). Gly emerges as the residue with the highest propensity to adopt C5 conformations, followed by Ser. Residues with branched sidechains Leu, Val and Ile are strongly disfavoured. Specific examples in protein structures that have contiguous residues in C5 conformations are highlighted.<\/jats:p>","DOI":"10.1002\/psc.70131","type":"journal-article","created":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T07:26:36Z","timestamp":1789802796000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Hydrogen Bonds Determining the Conformation of Isolated Amino Acid Residues in Proteins: Re\u2010Examination of the Fully Extended C5 Structures"],"prefix":"10.1002","volume":"32","author":[{"given":"Marimuthu","family":"Vijayasarathy","sequence":"first","affiliation":[{"name":"Prayoga Institute of Education Research  Bangalore India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6577-933X","authenticated-orcid":false,"given":"Padmanabhan","family":"Balaram","sequence":"additional","affiliation":[{"name":"National Centre for Biological Sciences Tata Institute of Fundamental Research  Bangalore India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,19]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.11.070142.000331"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1021\/cr60102a002"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja01452a015"},{"key":"e_1_2_8_5_1","volume-title":"The Nature of the Chemical Bond and the Structure of Molecules and Crystals: An Introduction to Modern Structural Chemistry","author":"Pauling L.","year":"1960"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1002\/anie.197101471"},{"key":"e_1_2_8_7_1","first-page":"321","article-title":"Polypeptide Chain Configurations in Crystalline Proteins","volume":"203","author":"Bragg W. 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