The Influenza M2 Cytoplasmic Tail Changes the Proton-Exchange Equilibria and the Backbone Conformation of the Transmembrane Histidine Residue to Facilitate Proton Conduction

Lignende værker

• NMR Detection of pH-Dependent Histidine-Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
  af: Hu, Fanghao, et al.
  Udgivet: (2011)
• Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel
  af: Williams, Jonathan K., et al.
  Udgivet: (2016)
• Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR
  af: Williams, Jonathan K., et al.
  Udgivet: (2017)
• Impact of Histidine Residues on the Transmembrane Helices of Viroporins
  af: Wang, Yan, et al.
  Udgivet: (2013)
• The Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State NMR
  af: Kwon, Byungsu, et al.
  Udgivet: (2016)