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  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. (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.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-C8C8-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-C8C9-6
Genre: Journal Article

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This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.
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https://dx.doi.org/10.1038/s41467-020-14971-0 (Publisher version)
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Miller, R. J. D.1, 2, Author              
Paré-Labrosse, O.1, 2, Author              
Sarracini, A.2, Author
Besaw, J. E.2, Author
Affiliations:
1Miller Group, Atomically Resolved Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_1938288              
2Departments of Chemistry and Physics, University of Toronto, ou_persistent22              

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 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?

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 Dates: 2019-11-182020-02-062020-03-06
 Publication Status: Published online
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 Rev. Type: Internal
 Identifiers: DOI: 10.1038/s41467-020-14971-0
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 11 (1) Sequence Number: 1240 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723