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Callaghan Innovation Research Papers

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TitleSub-Ångstrom structure of collagen model peptide (GPO)10 shows a hydrated triple helix with pitch variation and two proline ring conformations
Publication TypeJournal Article
Year of Publication2020
AuthorsSuzuki, H., Mahapatra D., Board A.J., Steel P.J., Dyer J.M., Gerrard J.A., Dobson R.C.J., and Valéry C.
JournalFood Chemistry
Volume319
Date Published2020
Keywordsacetic acid, amino acid sequence, article, Biomimetics, chemistry, Collagen, Collagen triple helix, Collagen-like peptides, Collagen-model peptide, controlled study, crystal structure, Crystal symmetry, Crystallography, X-Ray, electrospray mass spectrometry, food industry, glycine, Helical symmetry, Hierarchical assemblies, Hierarchical systems, high performance liquid chromatography, Hydration, hydrogen bond, Hydroxyproline, macrogol, Mammalian connective tissues, Mammals, Models, Molecular, molecular model, Musculoskeletal system, peptide fragment, Peptide Fragments, Peptides, proline, protein assembly, Protein Conformation, protein interaction, protein structure, Ring conformations, triple helix, Triple helixes, X ray crystallography
URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85081348961&doi=10.1016%2fj.foodchem.2020.126598&partnerID=40&md5=dc6ab612a22ec3d1f390a1bacaa59043
DOI10.1016/j.foodchem.2020.126598
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