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Journal Article

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

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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;

/persons/resource/persons93142

Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://www.sciencedirect.com/science/article/pii/002228369190554J/pdf?md5=c4a97e326081c8f9b557d70b9200a02d&pid=1-s2.0-002228369190554J-main.pdf
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https://doi.org/10.1016/0022-2836(91)90554-J
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Citation

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.


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