A high-resolution solid-state 13C-NMR study on [1-13C]Ala and [3-13C]Ala and [1-13C]Leu and Val-labelled bacteriorhodopsin. Conformation and dynamics of transmembrane helices, loops and termini, and hydration-induced conformational change-Reference-Cited by-同舟云学术

A high-resolution solid-state 13C-NMR study on [1-13C]Ala and [3-13C]Ala and [1-13C]Leu and Val-labelled bacteriorhodopsin. Conformation and dynamics of transmembrane helices, loops and termini, and hydration-induced conformational change

Published:1993-12 Issue:3 Volume:218 Page:837-844
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

TUZI Satoru,NAITO Akira,SAITO Hazime

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1993.tb18439.x/fullpdf

Reference43 articles.

1. Rhodopsin and bacteriorhodopsin: structure-function relationships

2. Bacteriorhodopsin and Related Pigments of Halobacteria

3. From Femtoseconds to Biology: Mechanism of Bacteriorhodopsin's Light-Driven Proton Pump

4. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin.

5. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy

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