CONFORMATIONAL FLEXIBILITY AND STRAND ARRANGEMENTS OF THE MEMBRANE-ASSOCIATED HIV FUSION PEPTIDE TRIMER PROBED BY SOLID-STATE NMR SPECTROSCOPY

Lignende værker

• Solid-State NMR Spectroscopy of Human Immunodeficiency Virus Fusion Peptides Associated with Host-Cell-Like Membranes: 2D Correlation Spectra and Distance Measurements Support a Fully Extended Conformation and Models for Specific Antiparallel Strand Registries
  af: Qiang, Wei, et al.
  Udgivet: (2008)
• Probing Single-Stranded DNA Conformational Flexibility Using Fluorescence Spectroscopy
  af: Murphy, M.C., et al.
  Udgivet: (2004)
• 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
  af: Sackett, Kelly, et al.
  Udgivet: (2013)
• 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
  af: Lee, Myungwoon, et al.
  Udgivet: (2018)
• The HIV Fusion Peptide and its Cross-Linked Oligomers: Efficient Syntheses, Significance of the Trimer in Fusion Activity, Correlation of β Strand Conformation with Membrane Cholesterol, and Proximity to Lipid Headgroups
  af: Qiang, Wei, et al.
  Udgivet: (2009)