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Article

Effects of two familial hypertrophic cardiomyopathy mutations in alpha-tropomyosin, Asp175Asn and Glu180Gly, on the thermal unfolding of actin-bound tropomyosin.

Biophysical journal - 1 Dec 2004

Kremneva Elena, Boussouf Sabrina, Nikolaeva Olga, Maytum Robin, Geeves Michael A, Levitsky Dmitrii I

Abstract excerpt

Differential scanning calorimetry was used to investigate the thermal unfolding of native alpha-tropomyosin (Tm), wild-type alpha-Tm expressed in Escherichia coli and the wild-type alpha-Tm carrying either of two missense mutations associated with familial hypertrophic cardiomyopathy, D175N or E180G. Recombinant alpha-Tm was expressed with an N-terminal Ala-Ser extension to substitute for the essential N-terminal...

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Source

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Identifiers

PMID: 15454401
DOI: 10.1529/biophysj.104.048793
PMCID: PMC1304903

Provenance

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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