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Article

Nuclear magnetic resonance characterization of peptide models of collagen-folding diseases.

Philosophical transactions of the Royal Society of London. Series B, Biological sciences - 28 Feb 2001

Buevich A, Baum J

Abstract excerpt

Misfolding of the triple helix has been shown to play a critical role in collagen diseases. The substitution of a single Gly by another amino acid breaks the characteristic repeating (Gly-X-Y)n sequence pattern and results in connective tissue disease such as osteogenesis imperfecta. Nuclear magnetic resonance (NMR) studies of normal and mutated collagen triple-helical peptides offer an opportunity to...

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Identifiers

PMID: 11260796
DOI: 10.1098/rstb.2000.0761
PMCID: PMC1088421

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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