Imidazole–Imidazole Hydrogen Bonding in the pH-Sensing Histidine Side Chains of Influenza A M2
Author:
Affiliation:
1. Department of NMR Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen 37077, Germany
Funder
Deutsche Forschungsgemeinschaft
Max-Planck-Gesellschaft
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
http://pubs.acs.org/doi/pdf/10.1021/jacs.9b10984
Reference48 articles.
1. Total Chemical Synthesis of the Integral Membrane Protein Influenza A Virus M2: Role of Its C-Terminal Domain in Tetramer Assembly
2. The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer
3. Structural characteristics of the M2 protein of influenza a viruses: Evidence that it forms a tetrameric channe
4. Specific structural alteration of the influenza haemagglutinin by amantadine.
5. Proton Association Constants of His 37 in the Influenza-A M218–60 Dimer-of-Dimers
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