Structure and protein environment of the retinal chromophore in light- and dark-adapted bacteriorhodopsin studied by solid-state NMR-Reference-Cited by-同舟云学术

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Structure and protein environment of the retinal chromophore in light- and dark-adapted bacteriorhodopsin studied by solid-state NMR

Published:1989-10 Issue:22 Volume:28 Page:8897-8904
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Smith Steven O.,De Groot Huub J. M.,Gebhard Ronald,Courtin Jacques M. L.,Lugtenburg Johan,Herzfeld Judith,Griffin Robert G.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00448a032

Reference41 articles.

1. Site of attachment of retinal in bacteriorhodopsin.

2. PHOTOPHYSICS OF LIGHT TRANSDUCTION IN RHODOPSIN AND BACTERIORHODOPSIN

3. Millisecond Fourier-transform infrared difference spectra of bacteriorhodopsin's M412 photoproduct.

4. Solid-state studies of some retinal iminium salts and related compounds: evidence for a 6-s-trans conformation

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