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Article

Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen.

American journal of medical genetics - 15 Jan 1993

Bächinger H P, Morris N P, Davis J M

Abstract excerpt

Osteogenesis imperfecta (OI) is an inherited disease in which 90% of the cases result from mutations in the 2 genes, pro alpha 1 and pro alpha 2, coding for type I collagen. Type I collagen is a trimeric molecule, (alpha 1)2 alpha 2, which is dominated both structurally and functionally by the 30...

Topics

Amino Acid Sequence
Animals
Collagen
Hot Temperature
Humans
Molecular Sequence Data
Mutation
Osteogenesis Imperfecta
Protein Folding

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 8456797
DOI: 10.1002/ajmg.1320450204

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8456797-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Thermal stability and folding of the collagen triple helix and the effects of mutations in osteogenesis imperfecta on the triple helix of type I collagen.PMID 8456797Read ↗

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

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 ↗

Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks.Semantic proximity Read ↗

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 ↗

Position of single amino acid substitutions in the collagen triple helix determines their effect on structure of collagen fibrils.Semantic proximity Read ↗

Disrupting Effects of Osteogenesis Imperfecta Mutations Could Be Predicted by Local Hydrogen Bonding Energy.Semantic proximity Read ↗

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

Type I collagen triplet duplication mutation in lethal osteogenesis imperfecta shifts register of alpha chains throughout the helix and disrupts incorporation of mutant helices into fibrils and extracellular matrix.Semantic proximity Read ↗

Thermostability gradient in the collagen triple helix reveals its multi-domain structure.Semantic proximity Read ↗

Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix.Semantic proximity Read ↗

Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine.Semantic proximity Read ↗

Predicting the clinical lethality of osteogenesis imperfecta from collagen glycine mutations.Semantic proximity Read ↗

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