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Effects of ATP analogs on the low-angle X-ray diffraction Pattern of insect flight muscle

MPG-Autoren
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Holmes,  Kenneth C.
Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

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Mannherz,  Hans Georg
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;

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Zitation

Barrington Leigh, J., Holmes, K. C., Mannherz, H. G., Rosenbaum, G., Eckstein, F., & Goody, R. S. (1973). Effects of ATP analogs on the low-angle X-ray diffraction Pattern of insect flight muscle. Cold Spring Harbor Symposia on Quantitative Biology, 27, 443-447. doi:10.1101/SQB.1973.037.01.055.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0019-B185-2
Zusammenfassung
Some years ago Reedy, Holmes, and Tregear (1965) noted that ATP had a dramatic effect upon the low-angle X-ray diffraction pattern of gly-cerinated fibers of the flight muscle from the giant water bug Lethocerus maximus. A strong meridional reflection appeared at a spacing of 145 A in the presence of ATP. When the ATP was washed out, this reflection disappeared and its place was taken by a 380 A layer line. With the help of electron microscopy these changes were shown to be due to an alteration in the orientation of the cross-bridges. In the absence of ATP (rigor state) the cross-bridges are at 45° to the filaments. In the presence of ATP the bridges appear to be free from the actin and are right-angled to the thick (myosin) filament (Fig. 1).