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

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 direct...

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Autores principales: R. J. Dwayne Miller, Olivier Paré-Labrosse, Antoine Sarracini, Jessica E. Besaw
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/ee99e130dfa442c4b1b664414387b56f
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spelling oai:doaj.org-article:ee99e130dfa442c4b1b664414387b56f2021-12-02T17:31:25ZThree-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance10.1038/s41467-020-14971-02041-1723https://doaj.org/article/ee99e130dfa442c4b1b664414387b56f2020-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14971-0https://doaj.org/toc/2041-1723How 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?R. J. Dwayne MillerOlivier Paré-LabrosseAntoine SarraciniJessica E. BesawNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-4 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
R. J. Dwayne Miller
Olivier Paré-Labrosse
Antoine Sarracini
Jessica E. Besaw
Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance
description 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?
format article
author R. J. Dwayne Miller
Olivier Paré-Labrosse
Antoine Sarracini
Jessica E. Besaw
author_facet R. J. Dwayne Miller
Olivier Paré-Labrosse
Antoine Sarracini
Jessica E. Besaw
author_sort R. J. Dwayne Miller
title Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance
title_short Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance
title_full Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance
title_fullStr Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance
title_full_unstemmed Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance
title_sort three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/ee99e130dfa442c4b1b664414387b56f
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