The excimer fluorescence of pyrene-labeled tropomyosin. A probe of conformational dynamics.
P Graceffa,Sherwin S. Lehrer +1 more
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TLDR
Rabbit skeletal and cardiac tropomyosin were specifically labeled at their cysteine side chains with N-(1-pyrene)-maleimide, indicating an inhibition of the salt-dependent polymerizability.About:
This article is published in Journal of Biological Chemistry.The article was published on 1980-12-10 and is currently open access. It has received 95 citations till now. The article focuses on the topics: Excimer.read more
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Supramolecular Hydrogelators and Hydrogels: From Soft Matter to Molecular Biomaterials
TL;DR: This review focuses on various potential applications of supramolecular hydrogels as molecular biomaterials, classified by their applications in cell cultures, tissue engineering, cell behavior, imaging, and unique applications of hydrogelators.
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THE Py SCALE OF SOLVENT POLARITIES. SOLVENT EFFECTS ON THE VIBRONIC FINE STRUCTURE OF PYRENE FLUORESCENCE and EMPIRICAL CORRELATIONS WITH ET and Y VALUES
Dao Cong Dong,Mitchell A. Winnik +1 more
TL;DR: In this paper, the I1/I3 values for pyrene fluorescence are suggested as the basis for a new empirical scale of solvent polarity, called the Py scale, which offers certain conveniences over other scales of solvent polarities.
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Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction.
TL;DR: The relation of protein structure to function will be emphasized and the relation of various physiologically and histochemically defined fiber types to the proteins found in them will be discussed.
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Pyrene: a probe to study protein conformation and conformational changes
TL;DR: The review focuses on the unique spectral features of pyrene that can be utilized to investigate protein structure and conformation as well as monitoring protein conformation, conformational changes, protein folding and unfolding, protein-protein,protein-lipid and protein-membrane interactions.
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Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase.
TL;DR: The results suggest a modification of the simple steric blocking theory of regulation, in which it is postulated that both of the Ca2+-dependent positions of tropomyosin on the thin filament block the formation of active acto-S1-nucleotide intermediates at low [S1], and in which tropomyOSin occupies a third "nonblocking" position in the active state at high [S2].
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Tropomyosin coiled-coil interactions: evidence for an unstaggered structure.
A.D. McLachlan,Murray Stewart +1 more
TL;DR: Stereochemical arguments based on models of the tropomyosin coiled-coil favour an unstaggered symmetrical form, since this allows the best packing of the hydrophobic groups on the inner face where the two helices interlock.
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Tropomyosin: a new asymmetric protein component of the muscle fibril.
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Troponin-tropomyosin complex. Column chromatographic separation and activity of the three, active troponin components with and without tropomyosin present.
Evan Eisenberg,W. Wayne Kielley +1 more
TL;DR: It is concluded that all three components plus tropomyosin are necessary to restore full Ca2+ sensitivity, and that this reconstitution can be accomplished by combining the individual components in the absence of urea.