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- W2000400771 abstract "The epimerization of amino acid residues increases with age in living organisms. In the present study, the structural consequences and thermodynamic functions of the epimerization of thymopentin (TP-5), the active site of the thymic hormone thymopoietin, were studied using molecular dynamics and density functional theory methods. The results show that free radical-initiated D-amino acid formation is energetically favoured (−130 kJmol−1) for each residue and induces significant changes to the peptide structure. In comparison to the wild-type (each residue in the L-configuration), the radius of gyration of the D-Asp3 epimer of the peptide decreased by 0.5 Å, and disrupted the intramolecular hydrogen bonding of the native peptide. Beyond establishing important structural, energetic and thermodynamic benchmarks and reference data for the structure of TP-5, these results disseminate the understanding of molecular ageing, the epimerization of amino acid residues." @default.
- W2000400771 created "2016-06-24" @default.
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- W2000400771 date "2014-05-23" @default.
- W2000400771 modified "2023-09-27" @default.
- W2000400771 title "Molecular ageing: Free radical initiated epimerization of thymopentin – A case study" @default.
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- W2000400771 doi "https://doi.org/10.1063/1.4871684" @default.
- W2000400771 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24880333" @default.
- W2000400771 hasPublicationYear "2014" @default.
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