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.
© (1992) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Richard D. Ludescher, Nano Mardones, 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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