{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T21:33:21Z","timestamp":1793223201699,"version":"4.5.0"},"reference-count":54,"publisher":"National Academy of Sciences","issue":"8","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2000,4,11]]},"abstract":"<jats:p>\n                    Mutations resulting in replacement of one obligate Gly residue within the repeating (Gly-Xaa-Yaa)\n                    <jats:sub>n<\/jats:sub>\n                    triplet pattern of the collagen type I triple helix are the major cause of osteogenesis imperfecta (OI). Phenotypes of OI involve fragile bones and range from mild to perinatal lethal. In this study, host\u2013guest triple-helical peptides of the form acetyl-(Gly-Pro-Hyp)\n                    <jats:sub>3<\/jats:sub>\n                    -\n                    <jats:italic>Zaa<\/jats:italic>\n                    -Pro-Hyp-(Gly-Pro-Hyp)\n                    <jats:sub>4<\/jats:sub>\n                    -Gly-Gly-amide are used to isolate the influence of the residue replacing Gly on triple-helix stability, with Zaa = Gly, Ala, Arg, Asp, Glu, Cys, Ser, or Val. Any substitution for Zaa = Gly (melting temperature,\n                    <jats:italic>T<\/jats:italic>\n                    <jats:sub>m<\/jats:sub>\n                    = 45\u00b0C) results in a dramatic destabilization of the triple helix. For Ala and Ser,\n                    <jats:italic>T<\/jats:italic>\n                    <jats:sub>m<\/jats:sub>\n                    decreases to \u224810\u00b0C, and for the Arg-, Val-, Glu-, and Asp-containing peptides,\n                    <jats:italic>T<\/jats:italic>\n                    <jats:sub>m<\/jats:sub>\n                    &lt; 0\u00b0C. A Gly \u2192 Cys replacement results in\n                    <jats:italic>T<\/jats:italic>\n                    <jats:sub>m<\/jats:sub>\n                    &lt; 0\u00b0C under reducing conditions but shows a broad transition (\n                    <jats:italic>T<\/jats:italic>\n                    <jats:sub>m<\/jats:sub>\n                    \u2248 19\u00b0C) in an oxidizing environment. Addition of trimethylamine\n                    <jats:italic>N<\/jats:italic>\n                    -oxide increases\n                    <jats:italic>T<\/jats:italic>\n                    <jats:sub>m<\/jats:sub>\n                    by \u22485\u00b0C per 1 M trimethylamine\n                    <jats:italic>N<\/jats:italic>\n                    -oxide, resulting in stable triple-helix formation for all peptides and allowing comparison of relative stabilities. The order of disruption of different Gly replacements in these peptides can be represented as Ala \u2264 Ser &lt; CPO\n                    <jats:sub>red<\/jats:sub>\n                    &lt; Arg &lt; Val &lt; Glu \u2264 Asp. The rank of destabilization of substitutions for Gly in these Gly-Pro-Hyp-rich homotrimeric peptides shows a significant correlation with the severity of natural OI mutations in the \u03b11 chain of type I collagen.\n                  <\/jats:p>","DOI":"10.1073\/pnas.070050097","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:35:07Z","timestamp":1027679707000},"page":"4273-4278","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":176,"title":["Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine"],"prefix":"10.1073","volume":"97","author":[{"given":"Konrad","family":"Beck","sequence":"first","affiliation":[{"name":"Department of Biochemistry, University of Medicine and Dentistry of New Jersey\u2013Robert Wood Johnson Medical School, Piscataway, NJ 08854; and CSIRO, Division of Molecular Science, Parkville, Victoria 3052, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Virginia C.","family":"Chan","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Medicine and Dentistry of New Jersey\u2013Robert Wood Johnson Medical School, Piscataway, NJ 08854; and CSIRO, Division of Molecular Science, Parkville, Victoria 3052, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nigel","family":"Shenoy","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Medicine and Dentistry of New Jersey\u2013Robert Wood Johnson Medical School, Piscataway, NJ 08854; and CSIRO, Division of Molecular Science, Parkville, Victoria 3052, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alan","family":"Kirkpatrick","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, University of Medicine and Dentistry of New Jersey\u2013Robert Wood Johnson Medical School, Piscataway, NJ 08854; and CSIRO, Division of Molecular Science, Parkville, Victoria 3052, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John A. 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