Ultraviolet Resonance Raman Evidence for the Opening of a Water-Permeable Channel in the M to N Transition of Bacteriorhodopsin-Reference-Cited by-同舟云学术

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Ultraviolet Resonance Raman Evidence for the Opening of a Water-Permeable Channel in the M to N Transition of Bacteriorhodopsin

Published:1998-01-01 Issue:2 Volume:120 Page:443-444
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Hashimoto Shinji¹,Sasaki Masato¹,Takeuchi Hideo¹

Affiliation:

1. Pharmaceutical Institute, Tohoku University Aobayama, Sendai 980-77, Japan

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja973187b

Reference28 articles.

Cited by 10 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Impact of protein–chromophore interaction on the retinal excited state and photocycle of Gloeobacter rhodopsin: role of conserved tryptophan residues;Chemical Science;2023

2. Probing Structure and Reaction Dynamics of Proteins Using Time-Resolved Resonance Raman Spectroscopy;Chemical Reviews;2019-12-09

3. Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy;Biochemistry;2015-07-29

4. Light-Induced Hydrolysis and Rebinding of Nonisomerizable Bacteriorhodopsin Pigment;Biophysical Journal;2002-05

5. Changes in Hydrogen Bonding and Environment of Tryptophan Residues on Helix F of Bacteriorhodopsin during the Photocycle: A Time-Resolved Ultraviolet Resonance Raman Study;Biochemistry;2002-04-27

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