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Article

Effects of troponin I phosphorylation on conformational exchange in the regulatory domain of cardiac troponin C.

The Journal of biological chemistry - 11 Jun 1999

Gaponenko V, Abusamhadneh E, Abbott M B, Finley N, Gasmi-Seabrook G, Solaro R J, Rance M, Rosevear P R

Abstract excerpt

Conformational exchange has been demonstrated within the regulatory domain of calcium-saturated cardiac troponin C when bound to the NH2-terminal domain of cardiac troponin I-(1-80), and cardiac troponin I-(1-80)DD, having serine residues 23 and 24 mutated to aspartate to mimic the phosphorylated form of the protein. Binding of cardiac troponin I-(1-80) decreases conformational exchange for residues 29, 32, and...

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Identifiers

PMID: 10358006
DOI: 10.1074/jbc.274.24.16681

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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