NMR Detection of pH-Dependent Histidine-Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel

Ítems similars

• Mechanisms of Proton Conduction and Gating in Influenza M2 Proton Channels from Solid-State NMR
  per: Hu, Fanghao, et al.
  Publicat: (2010)
• The Influenza M2 Cytoplasmic Tail Changes the Proton-Exchange Equilibria and the Backbone Conformation of the Transmembrane Histidine Residue to Facilitate Proton Conduction
  per: Liao, Shu Y., et al.
  Publicat: (2015)
• pH-Dependent Conformation, Dynamics, and Aromatic Interaction of the Gating Tryptophan Residue of the Influenza M2 Proton Channel from Solid-State NMR
  per: Williams, Jonathan K., et al.
  Publicat: (2013)
• Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel
  per: Williams, Jonathan K., et al.
  Publicat: (2016)
• Protonation equilibria and pore-opening structure of the dual-histidine influenza B virus M2 transmembrane proton channel from solid-state NMR
  per: Williams, Jonathan K., et al.
  Publicat: (2017)