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Article

1H NMR analysis of fibril-forming peptide fragments of transthyretin.

International journal of peptide and protein research - 1 Oct 1994

Jarvis J A, Kirkpatrick A, Craik D J

Abstract excerpt

Peptide fragments of the protein transthyretin, previously shown to form cross beta-sheet amyloid-like fibrils in vitro, were investigated using 1H 1D and 2D NMR techniques. TTR 10-20, TTR 105-115 as well as a substituted analogue, (TTR 105-115Met111) all formed amyloid-like fibrils readily in 20-30% acetonitrile/water at room temperature. It was found that the presence of fibrils in the peptide solutions did not...

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Source

Identifiers

PMID: 7875942
DOI: 10.1111/j.1399-3011.1994.tb01024.x

Genes

TTR

Provenance

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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1H NMR analysis of fibril-forming peptide fragments of transthyretin.PMID 7875942Read ↗

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Possible Existence of α-Sheets in the Amyloid Fibrils Formed by a TTR105-115 Mutant.Semantic proximity Read ↗

Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry.Semantic proximity Read ↗

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