Results 261 to 270 of about 5,264,822 (290)
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Journal of Molecular Biology, 1975
Abstract The structure of the actin-tropomyosin complex, which represents on active form of the thin filaments of skeletal muscle and the actin-tropomyosin-troponin T-troponin I complex, which represents an inhibited form, have been studied by three-dimensional reconstruction from electron micrographs.
T, Wakabayashi +3 more
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Abstract The structure of the actin-tropomyosin complex, which represents on active form of the thin filaments of skeletal muscle and the actin-tropomyosin-troponin T-troponin I complex, which represents an inhibited form, have been studied by three-dimensional reconstruction from electron micrographs.
T, Wakabayashi +3 more
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Biofizika, 2001
The method of fluorescence quenching was used to experimentally determine the distribution of tryptophan residues in molecules of troponin T, troponin T-troponin I complexes, and alpha-actinin. Iodide and cesium ions, and acrylamide were used as quenchers.
A G, Gvritishvili +6 more
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The method of fluorescence quenching was used to experimentally determine the distribution of tryptophan residues in molecules of troponin T, troponin T-troponin I complexes, and alpha-actinin. Iodide and cesium ions, and acrylamide were used as quenchers.
A G, Gvritishvili +6 more
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Human cardiac troponin complex. Structure and functions
Biochemistry (Moscow), 2013Troponin complex is a component of skeletal and cardiac muscle thin filaments. It consists of three subunits - troponin I, T, and C, and it plays a crucial role in muscle activity, connecting changes in intracellular Ca2+ concentration with generation of contraction.
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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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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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Structure of the insect troponin complex.
Journal of molecular biology, 1999Isolated troponin-tropomyosin complex from Lethocerus indicus asynchronous flight muscle forms paracrystals on a positively charged lipid monolayer. Single particle analysis was carried out on individual complexes selected from electron micrographs of negatively stained paracrystals.
T, Wendt, K, Leonard
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Extraction and Replacement of the Tropomyosin–Troponin Complex in Isolated Myofibrils
2010Tropomyosin (Tm) is an essential component in the regulation of striated muscle contraction. Questions about Tm functional role have been difficult to study because sarcomere Tm content is not as easily manipulated as Troponin (Tn). Here we describe the method we recently developed to replace Tm-Tn of skeletal and cardiac myofibrils from animals and ...
SCELLINI, BEATRICE +3 more
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Physarum Tropomyosin-Troponin Complex
The Journal of Biochemistry, 1975Toyoki KATO, Yuji TONOMURA
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Crosslinking of troponin complex with 1,3-difluoro-4,6-dinitrobenzene
BBA - Proteins and Proteomics, 1984N B Gusev, P Friedrich
exaly
Deciphering a macro-troponin I complex; a case report
Clinical Chemistry and Laboratory Medicine, 2017Richard Troughton +2 more
exaly

