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

R. J. Dwayne Miller (), Olivier Paré-Labrosse, Antoine Sarracini and Jessica E. Besaw
Additional contact information
R. J. Dwayne Miller: Max Planck Institute for the Structure and Dynamics of Matter
Olivier Paré-Labrosse: Max Planck Institute for the Structure and Dynamics of Matter
Antoine Sarracini: University of Toronto
Jessica E. Besaw: University of Toronto

Nature Communications, 2020, vol. 11, issue 1, 1-4

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?

Date: 2020
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-020-14971-0 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14971-0

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-020-14971-0

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().