Results 181 to 190 of about 27,067 (198)
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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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Tropomyosin and actin isoforms modulate the localization of tropomyosin strands on actin filaments
Journal of Molecular Biology, 2000Tropomyosin is present in virtually all eucaryotic cells, where it functions to modulate actin-myosin interaction and to stabilize actin filament structure. In striated muscle, tropomyosin regulates contractility by sterically blocking myosin-binding sites on actin in the relaxed state.
Robin Maytum +10 more
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The double helix of tropomyosin
Nature, 1975THE tropomyosin molecule consists of two α helices, which form a coiled-coil a little over 400 A long1. Besides forming crystals, tropomyosin can be precipitated with divalent cations to produce needle shaped aggregates (showing a variety of patterns of cross striations in the electron microscope2) for which the detailed molecular packings have not ...
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The tropomyosin mRNAs of mouse striated muscles: Molecular cloning of β-tropomyosin
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1988The nucleotide sequence corresponding to the complete coding region and much of the 5' and 3' untranslated regions of the skeletal muscle-specific mouse beta-tropomyosin mRNA was determined from overlapping cDNA clones isolated from a library of recombinants in pBR322.
David P. Leader, Colin McInnes
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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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Kinetics of folding and unfolding of αα‐tropomyosin and of nonpolymerizable αα‐tropomyosin
Biopolymers, 1991AbstractStopped flow CD (SFCD) kinetic studies of self–assembly of coiled coils of rabbit αα–tropomyosin and of nonpolymerizable αα–tropomyosin (NPTm) are reported. The protein was denatured in 6M urea buffer, then renatured by 10‐fold dilution into benign saline buffer. Folding was monitored by SFCD in the backbone region (222 nm).
Jianming Mo +2 more
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2008
Tropomyosins were discovered as regulators of actomyosin contractility in muscle cells, making yeasts and other fungi seem unlikely to harbor such proteins. Fungal cells are encased in a rigid cell wall and do not engage in the same sorts of contractile shape changes of animal cells.
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Tropomyosins were discovered as regulators of actomyosin contractility in muscle cells, making yeasts and other fungi seem unlikely to harbor such proteins. Fungal cells are encased in a rigid cell wall and do not engage in the same sorts of contractile shape changes of animal cells.
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Crystals of tropomyosin and native tropomyosin
Journal of Molecular Biology, 1968Sugie Higashi, Tatsuo Ooi
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The thermostability of tropomyosin
Biochemical and Biophysical Research Communications, 1965C.E. Bodwell +2 more
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