Results 271 to 280 of about 162,145 (312)
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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   +5 more
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Calmodulin as a model for troponin C

Biochemical and Biophysical Research Communications, 1980
Abstract 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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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.
J, Gergely, Z, Grabarek, T, Tao
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Defining the Region of Troponin-I that Binds to Troponin-C

Biochemistry, 1999
The kinetics and energetics of the binding of three troponin-I peptides, corresponding to regions 96-131 (TnI96-131), 96-139 (TnI96-139), and 96-148 (TnI96-148), to skeletal chicken troponin-C were investigated using multinuclear, multidimensional NMR spectroscopy.
R T, McKay   +4 more
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Calcium-induced flexibility changes in the troponin C–troponin I complex

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
The contraction of vertebrate striated muscle is modulated by Ca(2+) binding to the regulatory protein troponin C (TnC). Ca(2+) binding causes conformational changes in TnC which alter its interaction with the inhibitory protein troponin I (TnI), initiating the regulatory process.
X, Zhao   +6 more
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Interactions among chymotryptic troponin T subfragments, tropomyosin, troponin I and troponin C.

Journal of biochemistry, 1984
The binding of various combinations of chymotryptic troponin T subfragments, troponin I and troponin C to tropomyosin, troponin C and troponin I was examined semiquantitatively by using affinity chromatography. The interaction between troponin T2 and troponin I intensified the interaction between troponin T2 (or troponin T) and tropomyosin.
M, Tanokura, I, Ohtsuki
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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.
A P, Campbell, P J, Cachia, B D, Sykes
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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 ...
Y, Luo   +4 more
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Magnesium–Calcium Exchange in Cardiac Troponin C Bound to Cardiac Troponin I

Journal of Molecular and Cellular Cardiology, 2000
Understanding the process of Ca(2+)/Mg(2+)exchange during muscle excitation and relaxation is fundamental to elucidating the mechanism of Ca(2+)-regulated muscle contraction. During the resting phase, the C-domain of cardiac troponin C may be occupied by either Ca(2+)or Mg(2+).
N, Finley, A, Dvoretsky, P R, Rosevear
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Troponin C — Troponin I Interactions and Molecular Signalling in Cardiac Myofilaments

1995
This chapter describes a current perception of the molecular interactions regulating myofilament activity in heart cells. The focus is on the interaction between troponin-C (TnC), the Ca(2+)-receptor and troponin I (TnI), an inhibitory protein. It is this interaction that appears to form a molecular switch that turns on the thin filament.
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