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Cited by 279

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Chemical Dynamics in Proteins: The Photoisomerization of Retinal in Bacteriorhodopsin

Gai, Feng, Hasson, K. C., McDonald, J. Cooper, Anfinrud, Philip A.·1998·Science

Abstract

Chemical dynamics in proteins are discussed, with bacteriorhodopsin serving as a model system. Ultrafast time-resolved methods used to probe the chemical dynamics of retinal photoisomerization in bacteriorhodopsin are discussed, along with future prospects for ultrafast time-resolved crystallography. The photoisomerization of retinal in bacteriorhodopsin is far more selective and efficient than in solution, the origins of which are discussed in the context of a three-state model for the photoisomerization reaction coordinate. The chemical dynamics are complex, with the excited-state relaxation exhibiting a multiexponential decay with well-defined rate constants. Possible origins for the two major components are also discussed.

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Metadata

Authors
Gai, F., Hasson, K. C., McDonald, J. C., & Anfinrud, P. A.
Venue
Science
Published
1998-03-20
Volume
279
Issue
5358
Pages
1886-1891
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2059824119
Cited by
279
References
2
FWCI
4.70
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Chemical Dynamics in Proteins: The Photoisomerization of Retinal in Bacteriorhodopsin. https://app.cochat.ai/papers/10.1126/science.279.5358.1886
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Gai, F., Hasson, K. C., McDonald, J. C., & Anfinrud, P. A. (1998). Chemical Dynamics in Proteins: The Photoisomerization of Retinal in Bacteriorhodopsin. Science. https://doi.org/10.1126/science.279.5358.1886

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