The influenza fusion peptide promotes lipid polar head intrusion through hydrogen bonding with phosphates and N-terminal membrane insertion depth

Proteins: Structure, Function and Bioinformatics

Volumn 82, Issue 9, 2014, Pages 2118-2127

  Légaré, Sébastien ^a   Lagüe, Patrick ^a  

^a UNIVERSITÉ LAVAL   (Canada)

Author keywords

Lipid mixing; Lipid polar head intrusion; Lipid tail protrusion; Membrane fusion; Membrane peptide; Peptide N terminus lipid phosphate H bond

Indexed keywords

CARBON; INFLUENZA FUSION PEPTIDE; LIPID; MEMBRANE PROTEIN; PHOSPHATE; UNCLASSIFIED DRUG; VIRUS FUSION PROTEIN; HEMAGGLUTININ, HUMAN INFLUENZA A VIRUS; INFLUENZA VIRUS HEMAGGLUTININ; VIRUS PROTEIN;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; HYDROGEN BOND; LIPID POLAR HEAD INTRUSION; MEMBRANE FUSION; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTON NUCLEAR MAGNETIC RESONANCE; STATIC ELECTRICITY; CELL MEMBRANE; CHEMISTRY; GENETICS; HUMAN; INFLUENZA; INFLUENZA VIRUS A H3N2; METABOLISM; PHYSIOLOGY; VIROLOGY; VIRUS ATTACHMENT; VIRUS ENTRY;

CELL MEMBRANE; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; HUMANS; HYDROGEN BONDING; INFLUENZA A VIRUS, H3N2 SUBTYPE; INFLUENZA, HUMAN; LIPIDS; MEMBRANE FUSION; MOLECULAR DYNAMICS SIMULATION; PHOSPHATES; VIRAL FUSION PROTEINS; VIRAL TAIL PROTEINS; VIRUS ATTACHMENT; VIRUS INTERNALIZATION;

EID: 84906317081     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24568     Document Type: Article

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