Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR [Biophysics and Computational Biology]
Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR [Biophysics and Computational Biology]
Jakob Maciejko, Jagdeep Kaur, Johanna Becker-Baldus, Clemens Glaubitz...
Date: 2019-04-23
Proteorhodopsin (PR) is a highly abundant, pentameric, light-driven proton pump. Proton transfer is linked to a canonical photocycle typical for microbial ion pumps. Although the PR monomer is able to undergo a full photocycle, the question arises whether the pentameric complex formed in the membrane via specific cross-protomer interactions plays... Read More
PNAS:
Number: 17
Volume: 116
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b03606/20150713/images/medium/ja-2015-03606j_0008.gif
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[NMR paper] Visualizing specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by DNP-enhanced Solid-state NMR.
Visualizing specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by DNP-enhanced Solid-state NMR.
Visualizing specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by DNP-enhanced Solid-state NMR.
J Am Chem Soc. 2015 Jun 23;
Authors: Maciejko J, Mehler M, Kaur J, Lieblein T, Morgner N, Ouari O, Tordo P, Becker-Baldus J, Glaubitz C
Abstract
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Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR [Biophysics and Computational Biology]
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