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Journal ArticleDOI

Conformational change in actin filament induced by the interaction with heavy meromyosin: effects of pH, tropomyosin and deoxy-ATP.

Toshio Ando, +1 more
- 05 Apr 1979 - 
- Vol. 129, Iss: 2, pp 265-277
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TLDR
The conformational change in F-actin-TM induced by the interaction with HMM in the presence of deoxy-ATP has a long lifetime which continues for some time even after the detachment of the HMM.
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This article is published in Journal of Molecular Biology.The article was published on 1979-04-05. It has received 16 citations till now. The article focuses on the topics: Heavy meromyosin & Conformational change.

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Citations
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Journal ArticleDOI

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.
Journal ArticleDOI

Skeletal muscle myosin subfragment-1 induces bundle formation by actin filaments.

TL;DR: Fluorescence and electron microscopic observations of acto-S-1 solutions showed that super-opalescence results from formation of actin filament bundles once S-1 binds to F-actin.
Journal ArticleDOI

Perturbations of Functional Interactions with Myosin Induce Long-Range Allosteric and Cooperative Structural Changes in Actin †

TL;DR: The correlation of the perturbation-induced changes in TPA of actin with the functional effects suggests that the actomyosin interaction can be inhibited by stabilization ofActin in one of its structural intermediates.
Journal ArticleDOI

Fluorescence energy transfer between probes on actin and probes on myosin

TL;DR: Inter- and intramolecular distances strongly suggest that both the SH1 moiety and the ATPase site of myosin are located more than 6 nm from the actin sites.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
Journal ArticleDOI

Troponin. I. Preparation and physiological function.

TL;DR: In this article, a method for isolation of troponin from native tropomyosin was described, which was found to bind nearly 4 moles of Ca per 10 5 g, of which most were exchangeable.
Journal ArticleDOI

Meromyosins, the subunits of myosin

TL;DR: The isolation of the two subunits of myosin, obtained after short digestion by trypsin, were termed L- and H-meromyosins (“L” stands for light, “H” for heavy).
Journal Article

[Adenosine triphosphate, the functional group of actin].

TL;DR: In this paper, the importance of actin-bound ATP and its change during the change of form of the actin molecule is discussed in relation to the theory of muscle contraction, and the probable importance of protein-bound ADP in systems other than actin is discussed.
Journal ArticleDOI

Adenosinetriphosphate. The functional group of actin. 1950.

TL;DR: The importance of actin-bound ATP and its change during the change of form of the actin molecule is discussed in relation to the theory of muscle contraction and the probable importance of protein-bound ADP in systems other than actin is discussed.
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