Results 341 to 350 of about 19,854,960 (401)

Phosphorylation of troponin I by protein kinase C: Mechanism of inhibition by calmodulin and troponin C

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1987
The mechanism by which calmodulin and troponin C influence phosphorylation of troponin I (TnI) by protein kinase C was investigated. The phosphorylation of TnI by protein kinase C requires the presence of acidic phospholipid, calcium and diacylglycerol.
Paul D. Lampe, Gale M. Strasburg, Gary L. Nelsestuen, Mohammad D. Bazzi   +3 more
openaire   +3 more sources

Structural and functional studies on Troponin I and Troponin C interactions

Journal of Cellular Biochemistry, 2001
AbstractTroponin I (TnI) peptides (TnI inhibitory peptide residues 104–115, Ip; TnI regulatory peptide resides 1–30, TnI1–30), recombinant Troponin C (TnC) and Troponin I mutants were used to study the structural and functional relationship between TnI and TnC.
S M, Ngai, J R, Pearlstone, C S, Farah, F C, Reinach, L B, Smillie, R S, Hodges   +5 more
openaire   +3 more sources

The Molecular Switch in Troponin C

1993
Conformational changes in troponin C (TnC) associated with Ca(2+)-induced triggering of muscle contraction are discussed in light of the model proposed by Herzberg, Moult and James (J. Biol. Chem. 261, 2638, 1986) and of our recent work on mutants of troponin C.
John Gergely, Terence Tao, Zenon Grabarek   +2 more
openaire   +3 more sources

Extensive Interactions Between Troponins C and I. Zero-Length Footnotes: Crosslinking Of Troponin I and Acetylated Troponin C

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 ...
John H. Collins, John Gergely, Tomoyoshi Kobayashi, Zenon Grabarek   +3 more
openaire   +2 more sources

Functional and evolutionary relationships of troponin C [PDF]

Physiological Genomics, 2007
Striated 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, Glen F. Tibbits, Glen F. Tibbits, Christian R. Marshall   +3 more
openaire   +2 more sources

Interaction of troponin I and troponin C: ¹⁹F NMR studies of the binding of the inhibitory troponin I peptide to turkey skeletal troponin C

Biochemistry and Cell Biology, 1991
We have used 19F nuclear magnetic resonance spectroscopy to study the interaction of the inhibitory region of troponin (TnI) with apo- and calcium(II)-saturated turkey skeletal troponin C (TnC), using the synthetic TnI analogue Nα-acetyl[19FPhe106]TnI(104–115)amide.
Paul J. Cachia, Brian D. Sykes, A. Patricia Campbell   +2 more
openaire   +3 more sources

Proximity Relationships between Residue 6 of Troponin I and Residues in Troponin C:  Further Evidence for Extended Conformation of Troponin C in the Troponin Complex

Biochemistry, 2000
Skeletal muscle troponin C (TnC) adopts an extended conformation when crystallized alone and a compact one when crystallized with an N-terminal troponin I (TnI) peptide, TnI(1-47) [Vassylyev et al. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 4847-4852]. The N-terminal region of TnI (residues 1-40) was suggested to play a functional role of facilitating ...
John D. Leszyk, John Gergely, Bing Li, Yin Luo, Terence Tao   +4 more
openaire   +3 more sources

Melittin-Binding of Troponin C

The Journal of Biochemistry, 1993
Ca(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.
openaire   +3 more sources

Distance measurements in cardiac troponin C

Archives of Biochemistry and Biophysics, 1990
Intramolecular 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
openaire   +3 more sources

Calcium binding to cardiac troponin C

Archives of Biochemistry and Biophysics, 1978
Abstract 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, Ellen L. Kraft, Paul C. Leavis, Paul C. Leavis   +3 more
openaire   +3 more sources