Results 211 to 220 of about 18,693,880 (254)
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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.
C L, Wang, P C, Leavis
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Activation of troponin C by Cd2+ and Pb2+
Archives of Toxicology, 1990Certain heavy metal actions such as Cd2+ and Pb2+ mimic Ca2+ effectively in stimulating calmodulin (CaM). We now show that these cations also activate skeletal muscle troponin C (TnC), a Ca2(+)-binding protein highly homologous to CaM. Like Ca2+, these cations allow TnC to alter its electrophoretic mobility on polyacrylamide gels, and to bind to phenyl-
S H, Chao, C H, Bu, W Y, Cheung
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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. 1); one is expressed in fast
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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. 1); one is expressed in fast
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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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Binding of lanthanide ions to troponin C
Biochemistry, 1981Tb3+ and Eu3+ bound to troponin C were detected by (1) changes in the fluorescence of the tyrosine chromophore of the protein or (2) the luminescence of the ions themselves excited by energy transfer from the protein or by direct excitation using a pulsed laser light source [Horrocks, W. DeW., Jr., & Sudnick, D. R. (1979) Science (Washington, D.C.) 206,
C L, Wang +3 more
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Functional and evolutionary relationships of troponin C
Physiological Genomics, 2007Striated muscle contraction is initiated when, following membrane depolarization, Ca2+binds to the low-affinity Ca2+binding sites of troponin C (TnC). The Ca2+activation of this protein results in a rearrangement of the components (troponin I, troponin T, and tropomyosin) of the thin filament, resulting in increased interaction between actin and myosin
Todd E, Gillis +2 more
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