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Article

Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II.

Biochemistry - 22 Oct 1991

Brito R M, Putkey J A, Strynadka N C, James M N, Rosevear P R

Abstract excerpt

One- and two-dimensional NMR techniques were used to study both the influence of mutations on the structure of recombinant normal cardiac troponin C (cTnC3) and the conformational changes induced by Ca2+ binding to site II, the site responsible for triggering muscle contraction. Spin systems of the nine Phe and three Tyr residues were elucidated from DQF-COSY and NOESY spectra. Comparison of the pattern of NOE...

Topics

Animals
Calcium
Calcium-Binding Proteins
Chickens
Magnetic Resonance Spectroscopy
Mutation
Myocardium
Protein Conformation
Recombinant Proteins
Troponin
Troponin C

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Identifiers

PMID: 1931952
DOI: 10.1021/bi00106a023

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1931952-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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