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Article

Rotational and translational motion of troponin C.

The Journal of biological chemistry - 18 Jun 1999

Moncrieffe M C, Eaton S, Bajzer Z, Haydock C, Potter J D, Laue T M, Prendergast F G

Abstract excerpt

Time resolved fluorescence anisotropy and sedimentation velocity has been used to study the rotational and translational hydrodynamic behavior of two mutants of chicken skeletal troponin C bearing a single tryptophan residue at position 78 or 154 in the metal-free-, metal-bound-, and troponin I peptide (residues 96-116 of troponin I)-ligated states. The fluorescence anisotropy data of both mutants were adequately...

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Identifiers

PMID: 10364176
DOI: 10.1074/jbc.274.25.17464

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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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