{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["28(5)"],"submitter":["Joshi A"],"funding":["India Ministry of Science &amp; Technology Department of Biotechnology"],"pubmed_abstract":["Prolyl-4-hydroxylation is an ancient evolutionarily conserved post-translational modification (PTM) critical for both structural and regulatory functions in multicellular life forms. This PTM plays a pivotal role in stabilizing collagen's triple helix by influencing the puckering of the pyrrolidine ring. The elegant interplay between ring pucker, torsional angles, peptide bond isomerization, and charge-transfer interactions (O···C=O n→π∗ and σ→σ∗) attaining the helical stability remains underappreciated. Using density functional theory calibrated against gold standard <i>ab initio</i> methods, we analyzed a physiologically relevant collagenous peptide proline-4-hydroxyproline-glycine (PO<sup>4</sup>G) to establish the correlation between stereo-electronic effects due to prolyl-4-hydroxylat"],"journal":["iScience"],"pagination":["112393"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12059709"],"repository":["biostudies-literature"],"pubmed_title":["Decoding elegant interplay among different stereo-electronic effects due to the ancient prolyl-4-hydroxylation stabilizing collagenous helicity."],"pmcid":["PMC12059709"],"pubmed_authors":["Basak T","Mondal B","Joshi A"],"additional_accession":[]},"is_claimable":false,"name":"Decoding elegant interplay among different stereo-electronic effects due to the ancient prolyl-4-hydroxylation stabilizing collagenous helicity.","description":"Prolyl-4-hydroxylation is an ancient evolutionarily conserved post-translational modification (PTM) critical for both structural and regulatory functions in multicellular life forms. This PTM plays a pivotal role in stabilizing collagen's triple helix by influencing the puckering of the pyrrolidine ring. The elegant interplay between ring pucker, torsional angles, peptide bond isomerization, and charge-transfer interactions (O···C=O n→π∗ and σ→σ∗) attaining the helical stability remains underappreciated. Using density functional theory calibrated against gold standard <i>ab initio</i> methods, we analyzed a physiologically relevant collagenous peptide proline-4-hydroxyproline-glycine (PO<sup>4</sup>G) to establish the correlation between stereo-electronic effects due to prolyl-4-hydroxylat","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-01T05:23:30.378Z","creation":"2026-04-08T09:36:21.186Z"},"accession":"S-EPMC12059709","cross_references":{"pubmed":["40343281"],"doi":["10.1016/j.isci.2025.112393"]}}