Titlebook: Actin; Biophysics, Biochemi James E. Estes,Paul J. Higgins Book 1994 The Editor(s) (if applicable) and The Author(s), under exclusive licen

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Conclusions and Future Possibilities,ATP is also able to bind to actin in the actin:DNase I complex, suggesting that the nucleotide binding site in the actin:DNase I complex adopts a conformation similar to that found in F-actin. This result is consistent with the hypothesis that the two major domains of actin on either side of the cle

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https://doi.org/10.1007/978-3-031-32581-6le cells is essential to muscle contraction; the motile events of non-muscle cells involve active reorganization of the actin filament network. Actin has binding sites for one tightly bound divalent cation and one adenosine nucleotide per molecule. These ligands are important to the stability of the

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Types of Augmented Reality Systems,ods. Kerwar and Lehrer (1) were the first to demonstrate tryptophan fluorescence changes upon denaturation and polymerization of actin. We and others have made use of this work in assessing actin denaturation (2–4); however, intrinsic fluorescence has not been exploited as a general means of followi

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Nancy Baker Cahill,Jesse Damianievolution during ATP hydrolysis. Until now, driven by the availability of mutants. and atomic resolution structure of actin., the mapping of actomyosin interface has focused on the determination of myosin binding sites on actin. Two proximal areas on actin, in the N- and C-terminal regions of this p

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Springer Series on Cultural Computingre of energy, the tightly bound ATP being irreversibly hydrolyzed during polymerization. This dissipation of energy perturbs the laws of reversible helical polymerization defined by Oosawa and Asakura (1975), and affects the dynamics of actin filaments. We have shown that ATP hydrolysis destabilizes

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Springer Series on Cultural Computings and regulatory functions of tropomyosin have been extensively investigated. In addition, tropomyosin has served as a prototype for the structure of α-helical coiled-coil proteins (Cohen and Parry, 1990). The recent recognition of the diversity of tropomyosins in different cell types and discovery

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