Detection of Closed Influenza Virus Hemagglutinin Fusion Peptide Structures in Membranes by Backbone (13)CO-(15)N Rotational-Echo Double-Resonance Solid-State NMR

Gelijkaardige items

• Residue-Specific Membrane Location of Peptides and Proteins Using Specifically and Extensively Deuterated Lipids and 13C-2H Rotational-Echo Double-Resonance Solid-State NMR
  door: Xie, Li, et al.
  Gepubliceerd in: (2012)
• Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion Catalysis
  door: Ghosh, Ujjayini, et al.
  Gepubliceerd in: (2015)
• (2)H nuclear magnetic resonance spectroscopy supports larger amplitude fast motion and interference with lipid chain ordering for membrane that contains β sheet human immunodeficiency virus gp41 fusion peptide or helical hairpin influenza virus hemagglutinin fusion peptide at fusogenic pH
  door: Ghosh, Ujjayini, et al.
  Gepubliceerd in: (2020)
• Multiple Locations of Peptides in the Hydrocarbon Core of Gel-Phase Membranes Revealed by Peptide (13)C to Lipid (2)H Rotational-Echo Double-Resonance Solid-State Nuclear Magnetic Resonance
  door: Xie, Li, et al.
  Gepubliceerd in: (2014)
• Location of fluorotryptophan sequestered in an amphiphilic nanoparticle by rotational-echo double-resonance NMR.
  door: Baugher, A H, et al.
  Gepubliceerd in: (1998)