Results 291 to 300 of about 19,667,204 (333)
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.
Kazuhiro Yamada
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Biochemistry, 1992
We have quantitated the interactions of two rabbit skeletal troponin C fragments with troponin I and the troponin I inhibitory peptide. The calcium binding properties of the fragments and the ability of the fragments to exert control in the regulated actomyosin ATPase assay have also been studied. The N- and C-terminal divalent metal binding domains of
R. S. Fredricksen, Charles A. Swenson
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We have quantitated the interactions of two rabbit skeletal troponin C fragments with troponin I and the troponin I inhibitory peptide. The calcium binding properties of the fragments and the ability of the fragments to exert control in the regulated actomyosin ATPase assay have also been studied. The N- and C-terminal divalent metal binding domains of
R. S. Fredricksen, Charles A. Swenson
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Biochimica et Biophysica Acta (BBA) - Protein Structure, 1980
The stability of the structure of troponin C (calcium-binding components of troponin from rabbit skeletal muscle) has been studied by the scanning microcalorimetry method. It has been shows that: 1. In the presence of divalent ions the protein structure is represented by two practically independent cooperative blocks, one of which contains Ca2 ...
Tamara N. Tsalkova, Peter L. Privalov
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The stability of the structure of troponin C (calcium-binding components of troponin from rabbit skeletal muscle) has been studied by the scanning microcalorimetry method. It has been shows that: 1. In the presence of divalent ions the protein structure is represented by two practically independent cooperative blocks, one of which contains Ca2 ...
Tamara N. Tsalkova, Peter L. Privalov
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Nature, 1975
THE tropomyosin–troponin complex renders actomyosin from vertebrate skeletal muscle calcium sensitive. Troponin itself consists of three subunits: troponin I (TNI), troponin C (TNC) and troponin T (TNT)1. Pure TNI (24,000-dalton subunit) inhibits the actin–myosin interaction irrespective of calcium concentration.
James F. Head +3 more
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THE tropomyosin–troponin complex renders actomyosin from vertebrate skeletal muscle calcium sensitive. Troponin itself consists of three subunits: troponin I (TNI), troponin C (TNC) and troponin T (TNT)1. Pure TNI (24,000-dalton subunit) inhibits the actin–myosin interaction irrespective of calcium concentration.
James F. Head +3 more
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The mobility of troponin C and troponin I in muscle
Journal of Molecular Recognition, 1997In vertebrate skeletal muscle, contraction is initiated by the elevation of the intracellular Ca2+ concentration. The binding of Ca2+ to TnC induces a series of conformational changes which ultimately release the inhibition of the actomyosin ATPase activity by Tnl.
Kálmán Hideg +2 more
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Calmodulin as a model for troponin C
Biochemical and Biophysical Research Communications, 1980Abstract We have investigated the ability of calmodulin to replace troponin-C in the troponin complex. Unlike troponin-C, calmodulin is able to confer Ca 2+ -sensitivity on the actin-activated myosin subfragment-1 ATPase of filaments containing actin, tropomyosin and troponin-I in the absence of troponin-T. Gel electrophoresis of the supernatants and
CASTELLANI, Loriana +2 more
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Biochemistry and Cell Biology, 1998
The calcium-induced structural changes in the skeletal muscle regulatory protein troponin C involve a transition from a closed to an open structure with the concomitant exposure of a large hydrophobic interaction site for target proteins. NMR solution structural studies have served to define this conformational change and elucidate the mechanism of ...
Ryan T. McKay +3 more
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The calcium-induced structural changes in the skeletal muscle regulatory protein troponin C involve a transition from a closed to an open structure with the concomitant exposure of a large hydrophobic interaction site for target proteins. NMR solution structural studies have served to define this conformational change and elucidate the mechanism of ...
Ryan T. McKay +3 more
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The interaction of melittin with troponin C
Archives of Biochemistry and Biophysics, 1987Melittin has been found to interact with troponin C with high affinity in the presence of Ca2+. The association constant approaches in magnitude that for melittin and calmodulin. The interaction results in a shift to lower wavelengths of the emission band of Trp-19 of melittin and in an increased shielding of Trp-19 from quenching.
Lynn Norris, Robert F. Steiner
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Biochemistry, 2013
Troponin C (TnC) is the calcium-binding subunit of the troponin complex responsible for initiating striated muscle contraction in response to calcium influx.
Nicole M Cordina +5 more
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Troponin C (TnC) is the calcium-binding subunit of the troponin complex responsible for initiating striated muscle contraction in response to calcium influx.
Nicole M Cordina +5 more
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Crystallisation of troponin-C [PDF]
Nature, 1975 TROPONIN is the protein complex that controls the onset of muscular contraction1–3. It has three subunits4: troponin T (Tn-T), troponin I (Tn-I) and troponin C (Tn-C). The complex is bound at regular intervals along the thin filaments, which are composed of a double helix of actin monomers and tropomyosin, which runs along the grooves of the actin ...
Dan Mercola +2 more
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