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• W2004098469 abstract "Fluorescent ADP analog, ε-ADP (1:N6-ethenoadenosine 5′-diphosphate), was incorporated into F-actin in a myosin-free ghost single fiber and polarized fluorescence measurements were performed under a microspectrophotometer to investigate the conformation of F-actin and the changes induced in it by heavy meromyosin and subfragment-1. Four components of polarized fluorescence were obtained by exciting the fiber with light polarized parallel and perpendicular to the long axis of the fiber and measuring the intensity of emission polarized parallel and perpendicular. From these data it was shown that F-actin in the fiber was not rigid but flexible, with a value for the elastic modulus for bending of 5.3 × 10−17 dyn cm2. The angles of absorption dipole and emission dipole of bound ε-ADP with the long axis of F-actin were both about 75 °. The binding of heavy meromyosin decreased the elastic modulus of F-actin by 30% and the angles of absorption and emission dipoles by 2.5 ° and 1.5 °, respectively. The molar ratios of bound heavy meromyosin and subfragment-1 to actin in the ghost fiber at saturation were 0.3 and 0.6, respectively, being smaller than those in solution." @default.
• W2004098469 created "2016-06-24" @default.
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• W2004098469 date "1978-12-01" @default.
• W2004098469 modified "2023-10-13" @default.
• W2004098469 title "Polarized fluorescence from ε-ADP incorporated into F-actin in a myosin-free single fiber: Conformation of F-actin and hanges induced in it by heavy meromyosin" @default.
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• W2004098469 doi "https://doi.org/10.1016/0022-2836(78)90056-6" @default.
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