Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle state

Παρόμοια τεκμήρια

• 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
  ανά: Ratnayake, Punsisi U., κ.ά.
  Έκδοση: (2014)
• Hairpin Folding of HIV gp41 Abrogates Lipid Mixing Function at Physiologic pH and Inhibits Lipid Mixing by Exposed gp41 Constructs
  ανά: Sackett, Kelly, κ.ά.
  Έκδοση: (2009)
• HIV gp41 six-helix bundle constructs induce rapid vesicle fusion at pH 3.5 and little fusion at pH 7.0: understanding pH dependence of protein aggregation, membrane binding, and electrostatics, and implications for HIV-host cell fusion
  ανά: Sackett, Kelly, κ.ά.
  Έκδοση: (2011)
• Evidence That the Transition of HIV-1 Gp41 into a Six-Helix Bundle, Not the Bundle Configuration, Induces Membrane Fusion
  ανά: Melikyan, Grigory B., κ.ά.
  Έκδοση: (2000)
• Comparative analysis of membrane-associated fusion peptide secondary structure and lipid mixing function of HIV gp41 constructs which model the early pre-Hairpin intermediate and final Hairpin conformations
  ανά: Sackett, Kelly, κ.ά.
  Έκδοση: (2010)