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

Author

Listed:
  • R. J. Dwayne Miller

    (Max Planck Institute for the Structure and Dynamics of Matter
    University of Toronto)

  • Olivier Paré-Labrosse

    (Max Planck Institute for the Structure and Dynamics of Matter
    University of Toronto)

  • Antoine Sarracini

    (University of Toronto)

  • Jessica E. Besaw

    (University of Toronto)

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?

Suggested Citation

  • R. J. Dwayne Miller & Olivier Paré-Labrosse & Antoine Sarracini & Jessica E. Besaw, 2020. "Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance," Nature Communications, Nature, vol. 11(1), pages 1-4, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14971-0
    DOI: 10.1038/s41467-020-14971-0
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    Cited by:

    1. Quentin Bertrand & Przemyslaw Nogly & Eriko Nango & Demet Kekilli & Georgii Khusainov & Antonia Furrer & Daniel James & Florian Dworkowski & Petr Skopintsev & Sandra Mous & Isabelle Martiel & Per Börj, 2024. "Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate," Nature Communications, Nature, vol. 15(1), pages 1-11, December.

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