1 April 1992 Molecular dynamics of vertebrate muscle thick and thin filaments
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Abstract
Myosin-containing thick and actin-containing thin filaments generate force in vertebrate muscles. In an effort to monitor molecular dynamics and its relation to function in these filaments, we have labeled sulfhydryls actin (cys-374) and mysoin (SH1) with the triplet probe erythrosin-5-iodoacetamide. Fluorescence studies indicate that the probes are rigidly bound to the proteins and (probably) associated with the protein surface. Although the probe phosphorescence in solution is always mono-exponential, in the protein conjugates the decays are mono-exponential for actin but multiexponential for myosin at 20 degree(s)C. The steady- state anisotropy (averaged over the time window from 0.07 to 1.5 ms) of erythrosin-labeled G- actin is 0.0; in F-actin the anisotropy is 0.088 at 20 degree(s)C and increases to 0.10 when the peptide toxin phalloidin, which is known to stabilize F-actin filaments, is bound.
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Richard D. Ludescher, Richard D. Ludescher, Nano Mardones, Nano Mardones, Zane Liu, Zane Liu, } "Molecular dynamics of vertebrate muscle thick and thin filaments", Proc. SPIE 1640, Time-Resolved Laser Spectroscopy in Biochemistry III, (1 April 1992); doi: 10.1117/12.58260; https://doi.org/10.1117/12.58260
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