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  • Title: Actin-induced changes in the dynamics of myosin subfragment-1 detected by nuclear magnetic resonance.
    Author: Highsmith S, Jardetzky O.
    Journal: Ciba Found Symp; 1983; 93():156-8. PubMed ID: 6551227.
    Abstract:
    Analysis of high resolution 1H NMR spectra for myosin and myosin subfragment-1 (S-1) indicates that S-1 has an unusual structure, about 20% of which is mobile. The rest of the myosin molecule and F-actin are rigid by comparison. A wide variety of perturbations do not affect the S-1 internal mobility and suggest that the mobile structure is located in the interior of S-1. Actin binding uniquely quenches the internal motions entirely. The F and G forms have a similar effect. Nucleotide binding restores the internal motions under conditions known to cause dissociation of the acto-S-1 complex. A model of force generation by the actomyosin-nucleotide system, which incorporates this striking actin-induced change in S-1 structural dynamics, is proposed and discussed.
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