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  Imidazole-imidazole hydrogen bonding in the pH-sensing histidine side chains of influenza A M2.

Tekwani Movellan, K., Wegstroth, M., Overkamp, K., Leonov, A., Becker, S., & Andreas, L. B. (2020). Imidazole-imidazole hydrogen bonding in the pH-sensing histidine side chains of influenza A M2. Journal of the American Chemical Society, 142(6), 2704-2708. doi:10.1021/jacs.9b10984.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-93D2-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-BDE7-2
Genre: Journal Article

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 Creators:
Tekwani Movellan, K.1, Author              
Wegstroth, M.2, Author              
Overkamp, K.2, Author              
Leonov, A.2, Author              
Becker, S.2, Author              
Andreas, L. B.1, Author              
Affiliations:
1Research Group of Solid State NMR Spectroscopy-2, MPI for Biophysical Chemistry, Max Planck Society, ou_2396693              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 Abstract: The arrangement of histidine side chains in influenza A M2 tetramer determines their pKa values, which define pH-controlled proton conduction critical to the virus lifecycle. Both water-associated and hydrogen-bonded imidazole-imidazolium histidine quaternary structures have been proposed, based on crystal structures and NMR chemical shifts, respectively. Here we show, using the conduction domain construct of M2 in lipid bilayers, that the imidazole rings are hydrogen bonded even at a pH of 7.8 in the neutral charge state. An intermolecular 8.9 ± 0.3 Hz 2hJNN hydrogen bond is observed between H37 Nε and Nδ recorded in a fully protonated sample with 100 kHz magic-angle spinning. This interaction could not be detected in the drug-bound sample.

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Language(s): eng - English
 Dates: 2020-01-23
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/jacs.9b10984
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Title: Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: 142 (6) Sequence Number: - Start / End Page: 2704 - 2708 Identifier: -