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

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

    Research output: Contribution to journalArticle

    23 Citations (Scopus)

    Abstract

    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
    Volume262
    Issue number17
    Publication statusPublished - 1987 Jun 15

    Fingerprint

    Phosphorescence
    Myofibrils
    Anisotropy
    Myosins
    Cones
    Brownian movement
    Head
    Molecules

    ASJC Scopus subject areas

    • Biochemistry

    Cite this

    Rotational motions of myosin heads in myofibril studied by phosphorescence anisotropy decay measurements. / Ishiwata, S.; Kinosita, K.; Yoshimura, H.; Ikegami, A.

    In: Journal of Biological Chemistry, Vol. 262, No. 17, 15.06.1987, p. 8314-8317.

    Research output: Contribution to journalArticle

    Ishiwata, S, Kinosita, K, Yoshimura, H & Ikegami, A 1987, 'Rotational motions of myosin heads in myofibril studied by phosphorescence anisotropy decay measurements.', Journal of Biological Chemistry, vol. 262, no. 17, pp. 8314-8317.
    Ishiwata, S. ; Kinosita, K. ; Yoshimura, H. ; Ikegami, A. / Rotational motions of myosin heads in myofibril studied by phosphorescence anisotropy decay measurements. In: Journal of Biological Chemistry. 1987 ; Vol. 262, No. 17. pp. 8314-8317.
    @article{23c35fe1d2054b77be05993a9d46e6fe,
    title = "Rotational motions of myosin heads in myofibril studied by phosphorescence anisotropy decay measurements.",
    abstract = "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.",
    author = "S. Ishiwata and K. Kinosita and H. Yoshimura and A. Ikegami",
    year = "1987",
    month = "6",
    day = "15",
    language = "English",
    volume = "262",
    pages = "8314--8317",
    journal = "Journal of Biological Chemistry",
    issn = "0021-9258",
    publisher = "American Society for Biochemistry and Molecular Biology Inc.",
    number = "17",

    }

    TY - JOUR

    T1 - Rotational motions of myosin heads in myofibril studied by phosphorescence anisotropy decay measurements.

    AU - Ishiwata, S.

    AU - Kinosita, K.

    AU - Yoshimura, H.

    AU - Ikegami, A.

    PY - 1987/6/15

    Y1 - 1987/6/15

    N2 - 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.

    AB - 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.

    UR - http://www.scopus.com/inward/record.url?scp=0023655206&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=0023655206&partnerID=8YFLogxK

    M3 - Article

    C2 - 2439498

    AN - SCOPUS:0023655206

    VL - 262

    SP - 8314

    EP - 8317

    JO - Journal of Biological Chemistry

    JF - Journal of Biological Chemistry

    SN - 0021-9258

    IS - 17

    ER -