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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...

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Identifiers

PMID: 1931952
DOI: 10.1021/bi00106a023

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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