Results 301 to 310 of about 166,646 (357)
Some of the next articles are maybe not open access.
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1980
The stability of the structure of troponin C (calcium-binding components of troponin from rabbit skeletal muscle) has been studied by the scanning microcalorimetry method. It has been shows that: 1. In the presence of divalent ions the protein structure is represented by two practically independent cooperative blocks, one of which contains Ca2 ...
T N, Tsalkova, P L, Privalov
openaire +2 more sources
The stability of the structure of troponin C (calcium-binding components of troponin from rabbit skeletal muscle) has been studied by the scanning microcalorimetry method. It has been shows that: 1. In the presence of divalent ions the protein structure is represented by two practically independent cooperative blocks, one of which contains Ca2 ...
T N, Tsalkova, P L, Privalov
openaire +2 more sources
Nature, 1975
THE tropomyosin–troponin complex renders actomyosin from vertebrate skeletal muscle calcium sensitive. Troponin itself consists of three subunits: troponin I (TNI), troponin C (TNC) and troponin T (TNT)1. Pure TNI (24,000-dalton subunit) inhibits the actin–myosin interaction irrespective of calcium concentration.
R, Fine, W, Lehman, J, Head, A, Blitz
openaire +2 more sources
THE tropomyosin–troponin complex renders actomyosin from vertebrate skeletal muscle calcium sensitive. Troponin itself consists of three subunits: troponin I (TNI), troponin C (TNC) and troponin T (TNT)1. Pure TNI (24,000-dalton subunit) inhibits the actin–myosin interaction irrespective of calcium concentration.
R, Fine, W, Lehman, J, Head, A, Blitz
openaire +2 more sources
Biochemistry, 1992
We have quantitated the interactions of two rabbit skeletal troponin C fragments with troponin I and the troponin I inhibitory peptide. The calcium binding properties of the fragments and the ability of the fragments to exert control in the regulated actomyosin ATPase assay have also been studied. The N- and C-terminal divalent metal binding domains of
C A, Swenson, R S, Fredricksen
openaire +2 more sources
We have quantitated the interactions of two rabbit skeletal troponin C fragments with troponin I and the troponin I inhibitory peptide. The calcium binding properties of the fragments and the ability of the fragments to exert control in the regulated actomyosin ATPase assay have also been studied. The N- and C-terminal divalent metal binding domains of
C A, Swenson, R S, Fredricksen
openaire +2 more sources
Troponin T fragments: Physical properties and binding to troponin C
Canadian Journal of Biochemistry, 1978Fragments derived from rabbit skeletal troponin T (Tn-T) were tested for binding on a troponin C (Tn-C) – Sepharose affinity column in order to locate the binding site of Tn-C on Tn-T. The COOH-terminal fragments P2 (residues 159–209) and B2 (residues 206–258) were found to bind most strongly, confirming the earlier proposal (Pearlstone, J.
J R, Pearlstone, L B, Smillie
openaire +2 more sources
The mobility of troponin C and troponin I in muscle
Journal of Molecular Recognition, 1997In vertebrate skeletal muscle, contraction is initiated by the elevation of the intracellular Ca2+ concentration. The binding of Ca2+ to TnC induces a series of conformational changes which ultimately release the inhibition of the actomyosin ATPase activity by Tnl.
H C, Li, K, Hideg, P G, Fajer
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources