Structure transition in myosin association with the change of concentration: solubility equilibrium under specified KCl and pH condition

Biopolymers
Yoshisuke Tsunashima, Tohru Akutagawa

Abstract

We observed, for the first time, the elementary process for the ordered self-assembly formation of myosin in solution. It was realized exclusively under the specific condition of 200 mM KCl, 5 mM phosphate buffer, pH 7.08, at 15-20 degrees C, which is called the transition-generating condition (TGC). Described more in detail: pure myosin extracted from rabbit skeletal muscle exhibited the structural transition in its association form only when the myosin concentration c was changed under TGC. The myosin solubility was saturated in both edges of the total myosin concentration c > 10.0 mg/mL (solubility region II) and c < or = 0.25 mg/mL (solubility region I). In the intermediate region, the association structure of myosin changed stepwise with decreasing c. The steps were classified into four regions: region I (c < or = 0.25 mg/mL), II (0.25 < or = c < or = 0.50 mg/mL), III (0.50 < or = c < or = 5.0 mg/mL), and IV (c > 5.0 mg/mL). In each region except II, the plot of the relative soluble myosin concentration c(aq)/c against c(-1) gave a straight line of different slopes, certifying that myosin constructs self-assemblies by the closed association mechanism and that the self-assembly takes dual structures in each region. In regio...Continue Reading

References

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Citations

Oct 8, 2013·International Journal of Biological Macromolecules·Eisuke TakaiKentaro Shiraki
Nov 11, 2006·Proceedings of the National Academy of Sciences of the United States of America·Wulf BlankenfeldtIlme Schlichting
Dec 3, 2014·International Journal of Biological Macromolecules·Masato ShimadaKentaro Shiraki

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