An Insertion or Deletion in the Extramembrane Loop Connecting Helices E and F of Archaerhodopsin-1 Affects in vitro Refolding and Slows the Photocycle
Author:
Publisher
Wiley
Subject
Physical and Theoretical Chemistry,General Medicine,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1751-1097.1997.tb03186.x/fullpdf
Reference34 articles.
1. An Australian halobacterium contains a novel proton pump retinal protein: Archaerhodopsin
2. Isolation of a Gene That Encodes a New Retinal Protein, Archaerhodopsin, from Halobacterium sp. aus-1
3. Archaerhodopsin-2, from Halobacterium sp. aus-2 further reveals essential amino acid residues for light-driven proton pumps
4. AUSTRALIAN Halobacteria and THEIR RETINAL-PROTEIN ION PUMPS
5. pH DEPENDENCE OF THE ABSORPTION SPECTRA AND PHOTOCHEMICAL TRANSFORMATIONS OF THE ARCHAERHODOPSINS
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1. Two Consecutive Polar Amino Acids at the End of Helix E are Important for Fast Turnover of the Archaerhodopsin Photocycle;Photochemistry and Photobiology;2019-01-09
2. Over-Expression, Solubilization, and Purification of G Protein-Coupled Receptors for Structural Biology;Combinatorial Chemistry & High Throughput Screening;2008-07-01
3. The Effect of Carboxyl Group Modification on the Chromophore Regeneration of Archaeopsin-1 and Bacterioopsin;Journal of Biochemistry;1999-06-01
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