Results 261 to 270 of about 162,145 (312)
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Biochemistry, 1995
Interactions between troponin C (TnC) and troponin I (TnI) play an important role in the Ca(2+)-dependent regulation of vertebrate striated muscle contraction. Earlier studies have led to the proposal that the "inhibitory region" (residues 96-116) of TnI binds to an alpha-helical segment of TnC comprising residues 89-100 in the nonregulatory, C ...
T, Kobayashi +3 more
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Interactions between troponin C (TnC) and troponin I (TnI) play an important role in the Ca(2+)-dependent regulation of vertebrate striated muscle contraction. Earlier studies have led to the proposal that the "inhibitory region" (residues 96-116) of TnI binds to an alpha-helical segment of TnC comprising residues 89-100 in the nonregulatory, C ...
T, Kobayashi +3 more
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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.
C L, Wang, P C, Leavis
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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.
R F, Steiner, L, Norris
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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 ...
P C, Leavis, E L, Kraft
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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.
P C, Leavis, S S, Lehrer
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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.
Z, Grabarek, T, Tao, J, Gergely
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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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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 ...
S M, Gagné +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 ...
S M, Gagné +3 more
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The characterization of invertebrate troponin C
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1984TNCs from lobster, mussel, and squid migrated with rabbit TNC at an apparent mol. wt of 18,000. Electrophoretic mobilities in the presence or absence of Ca2+ were compared: the electrophoretic mobility of rabbit TNC was greater in the presence of Ca2+ than it its absence, but all invertebrate TNCs tested migrated identically, whether Ca2+ was present ...
Y, Shima +3 more
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1996
Abstract Troponin C (TnC) is an EF-hand Cal+-binding protein that is a constitutive subunit of the troponin complex on the thin filament of striated muscle. Cyclic binding and release of Cal• from the N-terminal Cal•-binding sites of TnC regulates muscle contraction. There are two isoforms of TnC (see Fig.
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Abstract Troponin C (TnC) is an EF-hand Cal+-binding protein that is a constitutive subunit of the troponin complex on the thin filament of striated muscle. Cyclic binding and release of Cal• from the N-terminal Cal•-binding sites of TnC regulates muscle contraction. There are two isoforms of TnC (see Fig.
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