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Time-resolved structural studies on insect flight muscle after photolysis of caged-ATP

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Rapp,  G.
Max Planck Institute for Medical Research, Max Planck Society;

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Poole,  Katrina J. V.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;
Abt. III: Strukturbiochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;
Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Citation

Rapp, G., Poole, K. J. V., Maeda, Y., Güth, K., Hendrix, J., & Goody, R. S. (1986). Time-resolved structural studies on insect flight muscle after photolysis of caged-ATP. Biophysical Journal, 50(5), 993-997. doi:10.1016/S0006-3495(86)83540-8.


Cite as: https://hdl.handle.net/21.11116/0000-0006-99B7-F
Abstract
The time course of structural changes occurring on ATP-induced relaxation of glycerinated insect flight muscle from the rigor state has been investigated using synchrotron radiation as a source of high intensity x rays and photolysis of caged-ATP to produce a rapid rise in ATP concentration. Temporal resolutions of 1 ms for the strongest equatorial reflections and 5 ms for the 14.5 nm meridional reflection are attainable from single events (i.e., without averaging over several cycles). The equatorial intensity changes completely, the meridional intensity partially, towards their respective relaxed values on a much faster time scale than relaxation of tension. The results suggest that actively cycling bridges present shortly after ATP-release are either too few in number to be detected in the equatorial diffraction pattern or that their structure is different from that of rigor bridges.