Results 311 to 320 of about 19,667,204 (333)
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Melittin-Binding of Troponin C
The Journal of Biochemistry, 1993Ca(2+)-dependent interaction between skeletal muscle troponin C and a bee venom melittin, which can be regarded as a mimic of the troponin C-binding peptide of troponin I, was investigated. Sephadex gel chromatography revealed that melittin bound to troponin C irrespective of the presence or absence of Ca2+ in 50 mM KCl and 50 mM Tris-HCl, pH 7.5.
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Distance measurements in cardiac troponin C
Archives of Biochemistry and Biophysics, 1990Intramolecular distance measurements were made in cardiac troponin C (cTnC) by fluorescence energy transfer using Eu3+ or Tb3+ as energy donors and Nd3+ or an organic chromophore as acceptors. The laser-induced luminescence of bound Eu3+ is quenched in Eu1Nd1cTnC with a lifetime of 0.328 ms, compared with 0.43 ms for Eu2cTnC.
Paul C. Leavis, Chih-Lueh Albert Wang
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Calcium binding to cardiac troponin C
Archives of Biochemistry and Biophysics, 1978Abstract The binding of Ca2+ to cardiac troponin C was studied by determining changes in the fluorescence and circular dichroism of the protein and by following changes in the free Ca2+ concentration by means of a Ca2+-specific electrode. Cardiac troponin C contains three Ca2+-binding sites which fall into two classes —two sites with a higher ...
Ellen L. Kraft+3 more
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Intrinsic fluorescence studies on troponin C
Archives of Biochemistry and Biophysics, 1978Abstract Evidence for a proton transfer mechanism in the Ca 2+ -induced enhancement of the Tyr fluorescence of troponin C was obtained by studying the effects, in D 2 O and H 2 O, of Ca 2+ , Mg 2+ , and H + on the fluorescence of both the protein and a model system containing L-Tyr in the presence of citrate.
Sherwin S. Lehrer+3 more
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Fluorescence dynamics studies of troponin C
Biopolymers, 1987AbstractThe time decay of fluorescence anisotropy for a dansylaziridine (DANZ) conjugate with Met‐25, which lies within the N‐terminal lobe of troponin C (TnC), shows at 10 and 25°C a longer correlation time characteristic of the entire molecule and a shorter correlation time arising from a more localized motion of the probe.
Lynn Norris, Robert F. Steiner
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Biochemistry, 1985
The refinement of the crystal structure of turkey skeletal muscle troponin C at 2.2-A resolution reveals that the two calcium binding loops that are occupied by Ca2+ ions adopt conformations very similar to those of the two homologous loops of ...
O. Herzberg, M. James
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The refinement of the crystal structure of turkey skeletal muscle troponin C at 2.2-A resolution reveals that the two calcium binding loops that are occupied by Ca2+ ions adopt conformations very similar to those of the two homologous loops of ...
O. Herzberg, M. James
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Molecular mechanism of troponin-C function
Journal of Muscle Research and Cell Motility, 1992There is now a large body of evidence in support of the view that Ca2+ binding to the low affinity sites of TnC induces a movement of helices B and C away from helices A and D, thus opening a hydrophobic cavity, the site of interaction with TnI. Another site of similar structure is formed by the helical segments in the C-terminal domain.
Terence Tao+4 more
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Peptide binding by calmodulin and its proteolytic fragments and by troponin C.
Biochemistry, 1984Calmodulin and troponin C exhibit calcium-dependent binding of 1 mol/mol of dynorphin. The dissociation constants of the complexes, determined in 0.20 N KC1-1.0 mM CaCI2, pH 7.3, are 0.6 microM for calmodulin, 2.4 microM for rabbit fast skeletal muscle ...
D. Malencik, S. Anderson
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Conformational Change of Troponin T Induced by Calcium Binding to Troponin C
The Journal of Biochemistry, 1985The 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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Calcium binding to troponin C and troponin: effects of Mg2+, ionic strength and pH.
Journal of Biochemistry (Tokyo), 1985Calcium binding to troponin C and troponin was examined by a metallochromic indicator method under various conditions to obtain a further understanding of the regulatory roles of these proteins in muscle contraction. Troponin C has four Ca binding sites,
Yasuo Ogawa
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