Results 311 to 320 of about 166,646 (357)

Molecular mechanism of troponin-C function

Journal of Muscle Research and Cell Motility, 1992
There 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
openaire   +2 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   +2 more sources

The NMR angle on troponin C

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, M X, Li, R T, McKay, B D, Sykes   +3 more
openaire   +2 more sources

The characterization of invertebrate troponin C

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1984
TNCs 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, T, Tsuchiya, W, Lehman, J J, Matsumoto   +3 more
openaire   +2 more sources

Troponin C

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.
openaire   +1 more source

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   +2 more sources

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, MORRIS E, AND O'BRIEN E. J.   +2 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.
J, Gergely, Z, Grabarek, T, Tao
openaire   +2 more sources

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, B P, Tripet, J R, Pearlstone, L B, Smillie, B D, Sykes   +4 more
openaire   +2 more sources

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, T, Kobayashi, Z, Gryczynski, I, Gryczynski, J, Lakowicz, R, Wade, J H, Collins   +6 more
openaire   +2 more sources