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Article

Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.

Biochemistry - 5 Apr 2016

Lim Kwang Hun, Dasari Anvesh K R, Hung Ivan, Gan Zhehong, Kelly Jeffery W, Wemmer David E

Abstract excerpt

Elucidation of structural changes involved in protein misfolding and amyloid formation is crucial for unraveling the molecular basis of amyloid formation. Here we report structural analyses of the amyloidogenic intermediate and amyloid aggregates of transthyretin using solution and solid-state nuclear magnetic resonance (NMR) spectroscopy. Our solution NMR results show that one of the two main β-sheet structures...

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Identifiers

PMID: 26998642
DOI: 10.1021/acs.biochem.6b00164
PMCID: PMC4904294

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Source receipt: pubmed, retrieved 7 Sept 2026.

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