Long-Range Effects on the Retinal Chromophore of Bacteriorhodopsin Caused by Surface Carboxyl Group Modification
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00024a011
Reference61 articles.
1. Surface charge of bacteriorhodopsin detected with covalently bound pH indicators at selected extracellular and cytoplasmic sites
2. The probable arrangement of the helices in G protein-coupled receptors.
3. Structure of the cell envelope of Halobacterium halobium.
4. Structure-function studies on bacteriorhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in Escherichia coli.
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1. Light adaptation of bacteriorhodopsin correlates with dielectric spectral kinetics in purple membrane;Biochemical and Biophysical Research Communications;2004-03
2. The Effect of Carboxyl Group Modification on the Chromophore Regeneration of Archaeopsin-1 and Bacterioopsin;Journal of Biochemistry;1999-06-01
3. Conformational change in bacterio-opsin on binding to retinal;Biophysical Chemistry;1999-04
4. The titrations of Asp-85 and of the cation binding residues in bacteriorhodopsin are not coupled;FEBS Letters;1999-03-26
5. Binding pathway of retinal to bacterio-opsin: a prediction by molecular dynamics simulations;Biophysical Journal;1997-12
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