Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin 
in the multiphoton regime and biological relevance

Miller, R. J. D.; Paré-Labrosse, O.; Sarracini, A.; Besaw, J. E.

doi:10.1038/s41467-020-14971-0

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Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance

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Miller, R. J. D.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Departments of Chemistry and Physics, University of Toronto;

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Paré-Labrosse, O.
Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Departments of Chemistry and Physics, University of Toronto;

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https://dx.doi.org/10.1038/s41467-020-14971-0
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Citation

Miller, R. J. D., Paré-Labrosse, O., Sarracini, A., & Besaw, J. E. (2020). Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance. Nature Communications, 11(1): 1240. doi:10.1038/s41467-020-14971-0.

Cite as: https://hdl.handle.net/21.11116/0000-0006-C8C8-7

Abstract

How does chemistry scale in complexity to unerringly direct biological functions? Nass Kovacs et al. have shown that bacteriorhodopsin undergoes structural changes tantalizingly similar to the expected pathway even under excessive excitation. Is the protein structure so highly evolved that it directs all deposited energy into the designed function?