Probing the Nature of the Blue-Shifted Intermediate of Photoactive Yellow Protein in Solution by NMR: Hydrogen−Deuterium Exchange Data and pH Studies-Reference-Cited by-同舟云学术

Probing the Nature of the Blue-Shifted Intermediate of Photoactive Yellow Protein in Solution by NMR: Hydrogen−Deuterium Exchange Data and pH Studies

Published:2000-10-28 Issue:47 Volume:39 Page:14392-14399
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Craven C. Jeremy¹,Derix Nocky M.¹,Hendriks Johnny¹,Boelens Rolf¹,Hellingwerf Klaas J.¹,Kaptein Robert¹

Affiliation:

1. Department of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands, and Department of Microbiology, E. C. Slater Institut, BioCentrum Amsterdam, University of Amsterdam, Nieuwe Achtergracht 127, 1018 WS Amsterdam, The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi001628p

Reference30 articles.

1. Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin

2. Structure of a Protein Photocycle Intermediate by Millisecond Time-Resolved Crystallography

3. Protein folding thermodynamics applied to the photocycle of the photoactive yellow protein

4. Structural and dynamic changes of photoactive yellow protein during its photocycle in solution

5. trans/cis (Z/E) photoisomerization of the chromophore of photoactive yellow protein is not a prerequisite for the initiation of the photocycle of this photoreceptor protein

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