Time-dependent absorption anisotropy and rotational diffusion of proteins in membranes.

S. Kawato, K. Kinosita

    Research output: Contribution to journalArticle

    56 Citations (Scopus)

    Abstract

    The decay of flash-induced absorption anisotropy, r(t), of a chromophore in a membrane protein is closely correlated with rotational diffusion of the protein in the membrane. We develop a theory of time-dependent absorption anisotropy which is applicable to both linear chromophores and planar chromophores which have two different absorption moments at right angles to one another. The theory treats two types of rotational diffusion of membrane proteins: one is rotation of the whole protein about the normal to the plane of the membrane, and the other is restricted wobbling of the whole or part of the protein molecule. In the former case, r(t) is determined by a rotational diffusion coefficient and an angle between the absorption moment(s) and the normal to the plane of the membrane. Rotation of rigid transmembrane proteins can be described by this treatment. In the latter case, r(t) is characterized by a wobbling diffusion coefficient and the degree of orientational constraint. This treatment may be applicable to independent wobbling of the hydrophilic part of membrane proteins. We further show that, for linear and circularly degenerate chromophores, the effect of the excitation flash intensity on r(t) can be accounted for by a constant scaling factor.

    Original languageEnglish
    Pages (from-to)277-296
    Number of pages20
    JournalBiophysical Journal
    Volume36
    Issue number1
    Publication statusPublished - 1981 Oct

    ASJC Scopus subject areas

    • Biophysics

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