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Q36348835-D1A5642C-BC76-43A8-9B2A-0A2BA3DE9858
Q36348835-D1A5642C-BC76-43A8-9B2A-0A2BA3DE9858
BestRank
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http://www.wikidata.org/entity/statement/Q36348835-D1A5642C-BC76-43A8-9B2A-0A2BA3DE9858
Dynamic Short Hydrogen Bonds in Histidine Tetrad of Full-Length M2 Proton Channel Reveal Tetrameric Structural Heterogeneity and Functional Mechanism
P2860
Q36348835-D1A5642C-BC76-43A8-9B2A-0A2BA3DE9858
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36348835-D1A5642C-BC76-43A8-9B2A-0A2BA3DE9858
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wasDerivedFrom
b0d829834f5337b2fa505d024165d70d72046b35
P2860
The influenza m2 cytoplasmic tail changes the proton-exchange equilibria and the backbone conformation of the transmembrane histidine residue to facilitate proton conduction