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...

Full description

Saved in:
Bibliographic Details
Published inNature communications Vol. 11; no. 1; p. 1240
Main Authors Miller, R. J. Dwayne, Paré-Labrosse, Olivier, Sarracini, Antoine, Besaw, Jessica E.
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 06.03.2020
Nature Publishing Group
Nature Portfolio
Subjects
140/125
631/45
631/535
631/57
639/638/439
639/638/45
Bacteriorhodopsin
Bacteriorhodopsins
Binding sites
Chemistry
Comment
Humanities and Social Sciences
Lasers
Motion pictures
multidisciplinary
Photons
Protein structure
Proteins
Retinaldehyde
Science
Science (multidisciplinary)
Online AccessGet full text

Cover

More Information
Summary: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?
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Commentary-1
ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-020-14971-0