Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity

Podobne zapisy

• Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations
  od: Kwon, Byungsu, i wsp.
  Wydane: (2020)
• Oligomeric Structure and Three-Dimensional Fold of the HIV gp41 MPER and Transmembrane Domain in Phospholipid Bilayers
  od: Kwon, Byungsu, i wsp.
  Wydane: (2018)
• The Influenza M2 Ectodomain Regulates the Conformational Equilibria of the Transmembrane Proton Channel: Insights from Solid-State NMR
  od: Kwon, Byungsu, i wsp.
  Wydane: (2016)
• Reversible Sheet–Turn Conformational Change of a Cell-Penetrating Peptide in Lipid Bilayers Studied by Solid-State NMR
  od: Su, Yongchao, i wsp.
  Wydane: (2008)
• Membrane-Dependent Conformation, Dynamics, and Lipid Interactions of the Fusion Peptide of the Paramyxovirus PIV5 from Solid-State NMR
  od: Yao, Hongwei, i wsp.
  Wydane: (2012)