title: Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO-          (15)N rotational-echo double-resonance solid-state NMR.
abstract: The influenza virus fusion peptide is the N-terminal ~20 residues of the HA2 subunit of the hemagglutinin protein and this peptide plays a key role in the fusion of the viral and endosomal membranes during initial infection of a cell. The fusion peptide adopts N-helix/turn/C-helix structure in both detergent and membranes with reports of both open and closed interhelical topologies. In the present study, backbone (13)CO-(15)N REDOR solid-state NMR was applied to the membrane-associated fusion peptide to detect the distribution of interhelical distances. The data clearly showed a large fraction of closed and semi-closed topologies and were best-fitted to a mixture of two structures that do not exchange. One of the earlier open structural models may have incorrect G13 dihedral angles derived from TALOS analysis of experimentally correct (13)C shifts.
authors: Department of Chemistry, Michigan State University, 578 S. Shaw Lane, East Lansing, MI 48824, USA.
authors: Ujjayini
authors: U
authors: Ghosh
authors: Li
authors: L
authors: Xie
authors: David P
authors: DP
authors: Weliky
mesh_terms: D000595:Amino Acid Sequence; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation
chemical_list: D019267:Hemagglutinin Glycoproteins, Influenza Virus; D010455:Peptides