Rotational motions of myosin heads in myofibril studied by phosphorescence anisotropy decay measurements.

S. Ishiwata*, K. Kinosita, H. Yoshimura, A. Ikegami

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    23 Citations (Scopus)


    We studied the rotational Brownian motions of myosin heads, of which the sulfhydryl group was selectively labeled with the triplet probe 5-eosinylmaleimide, in myofibril by using flash-induced phosphorescence anisotropy decay measurements. The anisotropy decay curve under relaxing conditions consisted of a fast (submicrosecond) and a slow (a few microseconds) component and a small constant part as in the synthetic myosin filaments in solution. The decay curves could be analyzed by assuming that a head part, i.e. subfragment 1 (S1), wobbles in the first cone and a part connecting S1 and the tail of a myosin molecule of which the length is shorter than subfragment 2 (S2) wobbles in the second cone (a double-cone model); the semiangles of the former and the latter cones were about 30 degrees and 50 degrees, respectively. The rotational freedom of myosin heads was only slightly restricted by the limited space of the filament lattice in myofibrils. Under rigor conditions, no motion of myosin heads was observed in the 10-microseconds time scale.

    Original languageEnglish
    Pages (from-to)8314-8317
    Number of pages4
    JournalJournal of Biological Chemistry
    Issue number17
    Publication statusPublished - 1987 Jun 15

    ASJC Scopus subject areas

    • Biochemistry


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