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Proceedings Paper

Molecular dynamics of vertebrate muscle thick and thin filaments
Author(s): Richard D. Ludescher; Nano Mardones; Zane Liu
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Paper 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.

Paper Details

Date Published: 1 April 1992
PDF: 7 pages
Proc. SPIE 1640, Time-Resolved Laser Spectroscopy in Biochemistry III, (1 April 1992); doi: 10.1117/12.58260
Show Author Affiliations
Richard D. Ludescher, Rutgers Univ. (United States)
Nano Mardones, Rutgers Univ. (United States)
Zane Liu, Rutgers Univ. (United States)

Published in SPIE Proceedings Vol. 1640:
Time-Resolved Laser Spectroscopy in Biochemistry III
Joseph R. Lakowicz, Editor(s)

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