Time-resolved cryo-electron microscopic study of the dissociation of actomyosin 
induced by photolysis of photolabile nucleotides

Menetret, J. F.; Hofmann, W. F.; Schröder, Rasmus R.; Rapp, Gert; Goody, Roger S.

doi:10.1016/0022-2836(91)90554-J

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Time-resolved cryo-electron microscopic study of the dissociation of actomyosin induced by photolysis of photolabile nucleotides

MPS-Authors

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Schröder, Rasmus R.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
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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https://www.sciencedirect.com/science/article/pii/002228369190554J/pdf?md5=c4a97e326081c8f9b557d70b9200a02d&pid=1-s2.0-002228369190554J-main.pdf
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引用

Menetret, J. F., Hofmann, W. F., Schröder, R. R., Rapp, G., & Goody, R. S. (1991). Time-resolved cryo-electron microscopic study of the dissociation of actomyosin induced by photolysis of photolabile nucleotides. Journal of Biological Chemistry, 219(2), 139-144. doi:10.1016/0022-2836(91)90554-J.

引用: https://hdl.handle.net/11858/00-001M-0000-0019-ACCD-4

要旨

The rapid release of a substrate or other ligand from photolabile precursors in a thin layer suspension of biological specimens followed by rapid freezing provides a method of trapping and visualizing short-lived states in a dynamic system. We demonstrate here the first successful application of this method to study the interaction of actin filaments with myosin subfragment 1 (S1) after release of nucleotides. The results obtained suggest that structural changes in actin filaments occur as a result of interaction with S1.