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Article

Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta.

Biopolymers - 1 Jan 2011

Bryan Michael A, Cheng Haiming, Brodsky Barbara

Abstract excerpt

Osteogenesis imperfecta (OI), a disorder characterized by fragile bones, is often a consequence of missense mutations in type I collagen, which change one Gly in the repeating (Gly-Xaa-Yaa)(n) sequence to a larger amino acid. The impact of local environment and the identity of the residue replacing Gly were investigated using two sets of triple-helical peptides. Gly mutations in the highly stable...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 20235194
DOI: 10.1002/bip.21432
PMCID: PMC2980582

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta.PMID 20235194Read ↗

Osteogenesis Imperfecta Missense Mutations in Collagen: Structural Consequences of a Glycine to Alanine Replacement at a Highly Charged SiteSemantic proximity Read ↗

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Recombinant collagen studies link the severe conformational changes induced by osteogenesis imperfecta mutations to the disruption of a set of interchain salt bridges.Semantic proximity Read ↗

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Substitutions for arginine at position 780 in triple helical domain of the α1(I) chain alter folding of the type I procollagen molecule and cause osteogenesis imperfecta.Semantic proximity Read ↗

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