Results 221 to 230 of about 18,693,880 (254)
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Interaction of a troponin I inhibitory peptide with both domains of troponin C

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996
Skeletal muscle contraction is regulated by Ca2+ binding to troponin (Tn), a complex of three proteins attached to the actin-tropomyosin filaments. We have been investigating key interactions of the Ca(2+)-binding protein TnC and the inhibitory protein TnI.
T, Kobayashi, P C, Leavis, J H, Collins
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Comparison of the Kinetic Properties of Troponin-C and Dansylaziridine-Labeled Troponin-C1

The Journal of Biochemistry, 1980
Comparison of the kinetic properties of troponin-C and dansylaziridine-labeled troponin-C revealed that the calcium ion binding and removal reactions with the low affinity Ca2+-binding sites (sites I and II) and the resultant local conformational change are rapid processes, and that the calcium ion binding and removal reactions with the high affinity ...
T, Iio, H, Kondo
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The enthalpy titration of troponin C with calcium

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1978
Microcalorimetric titrations have been used to study the binding of Ca2+ to troponin C, the Ca-binding component of troponin. Troponin C was extracted from rabbit skeletal muscle and Ca2+ was added to Ca-free troponin C in the presence of 1 mM Mg2+ at pH 8.83 at 10 degrees C.
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Interaction of troponin I and troponin C

Journal of Molecular Biology, 1991
A.Patricia Campbell, Brian D. Sykes
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Conformational Change of Troponin T Induced by Calcium Binding to Troponin C

The Journal of Biochemistry, 1985
The skeletal muscle troponin complex, the troponin T subunit of which was labeled with 2-((4'-iodoacetamido)anilino)naphthalene-6-sulfonic acid, showed a fluorescence titration curve with a midpoint of around pCa 6.75. Addition of 2 mM MgCl2 had no effect on the fluorescence titration curve.
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Troponin C — Troponin I Interactions and Molecular Signalling in Cardiac Myofilaments

1995
This chapter describes a current perception of the molecular interactions regulating myofilament activity in heart cells. The focus is on the interaction between troponin-C (TnC), the Ca(2+)-receptor and troponin I (TnI), an inhibitory protein. It is this interaction that appears to form a molecular switch that turns on the thin filament.
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Cardiac Troponin T and Troponin I in the General Population

Circulation, 2019
Claire Welsh   +2 more
exaly  

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