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Partial solid-state NMR 1H, 13C, 15N resonance assignments of a perdeuterated back-exchanged seven-transmembrane helical protein Anabaena Sensory Rhodopsin

Partial solid-state NMR 1H, 13C, 15N resonance assignments of a perdeuterated back-exchanged... Anabaena Sensory Rhodopsin (ASR) is a unique photochromic membrane-embedded photosensor which interacts with soluble transducer and is likely involved in a light-dependent gene regulation in the cyanobacterium Anabaena sp. PCC 7120. We report partial spectroscopic 1H, 13C and 15N assignments of perdeuterated and back-exchanged ASR reconstituted in lipids. The reported assignments are in general agreement with previously determined assignments of carbon and nitrogen resonances in fully protonated samples. Because the back-exchange was performed on ASR in a detergent-solubilized state, the location of detected residues reports on the solvent accessibility of ASR in detergent. A comparison with the results of previously published hydrogen/exchange data collected on the ASR reconstituted in lipids, suggests that the protein has larger solvent accessible surface in the detergent-solubilized state. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

Partial solid-state NMR 1H, 13C, 15N resonance assignments of a perdeuterated back-exchanged seven-transmembrane helical protein Anabaena Sensory Rhodopsin

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References (32)

Publisher
Springer Journals
Copyright
Copyright © 2018 by Springer Science+Business Media B.V., part of Springer Nature
Subject
Physics; Biological and Medical Physics, Biophysics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-018-9815-6
Publisher site
See Article on Publisher Site

Abstract

Anabaena Sensory Rhodopsin (ASR) is a unique photochromic membrane-embedded photosensor which interacts with soluble transducer and is likely involved in a light-dependent gene regulation in the cyanobacterium Anabaena sp. PCC 7120. We report partial spectroscopic 1H, 13C and 15N assignments of perdeuterated and back-exchanged ASR reconstituted in lipids. The reported assignments are in general agreement with previously determined assignments of carbon and nitrogen resonances in fully protonated samples. Because the back-exchange was performed on ASR in a detergent-solubilized state, the location of detected residues reports on the solvent accessibility of ASR in detergent. A comparison with the results of previously published hydrogen/exchange data collected on the ASR reconstituted in lipids, suggests that the protein has larger solvent accessible surface in the detergent-solubilized state.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Mar 23, 2018

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