Results 301 to 310 of about 76,365 (337)
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1999
Abstract Tropomyosins (TMs) are found in virtually all eukaryotic cells in association with actin. In skeletal and cardiac muscles, TM, together with the troponin complex, comprises the regulatory mechanism by which the interaction of F-actin and myosin are controlled by the level of calcium ions,3,4 In smooth muscle and non-muscle cells
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Abstract Tropomyosins (TMs) are found in virtually all eukaryotic cells in association with actin. In skeletal and cardiac muscles, TM, together with the troponin complex, comprises the regulatory mechanism by which the interaction of F-actin and myosin are controlled by the level of calcium ions,3,4 In smooth muscle and non-muscle cells
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Crystalline sheets of tropomyosin
Journal of Molecular Biology, 1984In the presence of spermine tropomyosin forms sheets having two-dimensional crystallinity and tactoids. The most common form of sheet has cmm symmetry with a = 80 nm and b = 5 nm. The structure of this sheet has been solved in projection to a nominal resolution of 1.5 nm by combining data from electron diffraction and electron microscopy.
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Tropomyosin-troponin and tropomyosin-actin interactions: a fluorescence quenching study
Biochemistry, 1983Rabbit skeletal alpha alpha-tropomyosin was specifically labeled at Cys-190 with the fluorescent probe N-(iodoacetyl)-N'-(1-naphthyl-5-sulfo)ethylenediamine (1,5-IAE-DANS). The fluorescence decay of the resultant AE-DANS-labeled alpha alpha-tropomyosin (Tm) was monoexponential with a lifetime of 13.55 ns.
M, Lamkin, T, Tao, S S, Lehrer
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Structure of Molluscan Tropomyosin
Nature, 1957CERTAIN molluscan smooth muscles contain protein filaments with a regular and characteristic fine structure1–3 to which the name paramyosin has been given4. Neither the chemical nature nor the function of these filaments is understood, and attention is once more drawn to these problems by the recent discovery in the same muscles of an asymmetric ...
J, HANSON +5 more
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Calponin and tropomyosin interactions
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992The interaction between chicken gizzard calponin and tropomyosin was examined using viscosity, light scattering, electron microscopy and affinity chromatography. At neutral pH, 10 mM NaCl and in the absence of Mg2+, calponin induced tropomyosin filaments to form paracrystals thus decreasing the viscosity while increasing dramatically the light ...
T J, Childs +4 more
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Isoform Sorting of Tropomyosins
2008Cytoskeletal tropomyosin (Tm) isoforms show extensive intracellular sorting, resulting in spatially distinct actin-filament populations. Sorting of Tm isoforms has been observed in a number of cell types, including fibroblasts, epithelial cells, osteoclasts, neurons and muscle cells.
Claire, Martin, Peter, Gunning
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Tropomyosin: Function Follows Structure
2008Tropomyosin is known as the archetypal coiled coil, being the first to be sequenced and modeled. Studies of the structure and dynamics of tropomyosin, accompanied by biochemical and biophysical analyses of tropomyosin, mutants and model peptides, have revealed the complexity and subtleties required for tropomyosin function.
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Tropomyosin and molecular mimicry
Parasitology Today, 1991cyst investiture in nonmuscle tropo- myosin may play a role in immune evasion in the snail host by protecting the sporocyst from amoebocyte attack. If true, this would be a prime example of molecular mimicry in its full and original sense s , which links common structures to the host-parasite relationship.
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Nature, 1965
THIS communication reports the determination of the molecular weight of rabbit tropomyosin by equilibrium sedimentation in a solvent consisting of 8 M urea, 0.2 M sodium chloride, 0.025 M sodium dihydrogen phosphate adjusted to pH. 7.0, and 0.1 M β-mercaptoethanol.
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THIS communication reports the determination of the molecular weight of rabbit tropomyosin by equilibrium sedimentation in a solvent consisting of 8 M urea, 0.2 M sodium chloride, 0.025 M sodium dihydrogen phosphate adjusted to pH. 7.0, and 0.1 M β-mercaptoethanol.
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