Stabilities of the Soluble Ectodomain and Fusion Peptide Hairpins of the Influenza Virus Hemagglutinin Subunit II Protein Are Positively-Correlated with Membrane Fusion

Eitemau Tebyg

• Hydrogen-deuterium exchange supports independent membrane-interfacial fusion peptide and transmembrane domains in subunit 2 of influenza virus hemagglutinin protein, a structured and aqueous-protected connection between the fusion peptide and soluble ectodomain, and the importance of membrane apposition by the trimer-of-hairpins structure
  gan: Ranaweera, Ahinsa, et al.
  Cyhoeddwyd: (2019)
• Full-Length Trimeric Influenza Virus Hemagglutinin II Membrane Fusion Protein and Shorter Constructs Lacking the Fusion Peptide or Transmembrane Domain: Hyperthermostability of the Full-Length Protein and the Soluble Ectodomain and Fusion Peptide Make Significant Contributions to Fusion of Membrane Vesicles()
  gan: Ratnayake, Punsisi U., et al.
  Cyhoeddwyd: (2015)
• pH-Dependent Vesicle Fusion Induced by the Ectodomain of the Human Immunodeficiency Virus Membrane Fusion Protein gp41: Two Kinetically Distinct Processes and Fully-Membrane-Associated gp41 with Predominant β Sheet Fusion Peptide Conformation
  gan: Ratnayake, Punsisi U., et al.
  Cyhoeddwyd: (2014)
• Folded Monomers and Hexamers of the Ectodomain of the HIV gp41 Membrane Fusion Protein: Potential Roles in Fusion and Synergy Between the Fusion Peptide, Hairpin, and Membrane-Proximal External Region
  gan: Banerjee, Koyeli, et al.
  Cyhoeddwyd: (2014)
• Helical Hairpin Structure of Influenza Hemagglutinin Fusion Peptide Stabilized by Charge-Dipole Interactions between the N-terminal Amino Group and the Second Helix
  gan: Lorieau, Justin L., et al.
  Cyhoeddwyd: (2011)