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Article

A proton nuclear magnetic resonance and molecular modeling study of cardiac troponin C. Calcium dependence and aromatic spectral assignments.

The Journal of biological chemistry - 15 Jun 1990

MacLachlan L K, Reid D G, Carter N

Abstract excerpt

Proton (1H) NMR at 360 MHz has been used to characterize calcium-induced spectral changes in bovine cardiac troponin C in more detail than hitherto reported (Hincke, M. T., Sykes, B. D., and Kay, C. M. (1981) Biochemistry 20, 3286-3294). The observed changes are consistent with two equivalents of calcium occupying high affinity sites, with subsequent binding of a single equivalent to a lower affinity site....

Topics

Amino Acid Sequence
Animals
Binding Sites
Calcium
Cattle
Hydrogen
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Mutation
Myocardium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Protein Conformation

Software

Troponin

Troponin C

Source

Identifiers

PMID: 2351671

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2351671-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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A proton nuclear magnetic resonance and molecular modeling study of cardiac troponin C. Calcium dependence and aromatic spectral assignments.PMID 2351671Read ↗

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Probing the relationship between alpha-helix formation and calcium affinity in troponin C: 1H NMR studies of calcium binding to synthetic and variant site III helix-loop-helix peptides.Semantic proximity Read ↗

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Allosteric Transmission along a Loosely Structured Backbone Allows a Cardiac Troponin C Mutant to Function with Only One Ca2+ Ion.Semantic proximity Read ↗

The structure of cardiac troponin C regulatory domain with bound Cd2+ reveals a closed conformation and unique ion coordination.Semantic proximity Read ↗

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Hypertrophic cardiomyopathy-linked mutation D145E drastically alters calcium binding by the C-domain of cardiac troponin C.Semantic proximity Read ↗

Mutations in the N- and D-helices of the N-domain of troponin C affect the C-domain and regulatory function.Semantic proximity Read ↗

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