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Volumn 277, Issue 25, 2002, Pages 22725-22733
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Structural characterizations of fusion peptide analogs of influenza virus hemagglutinin. Implication of the necessity of a helix-hinge-helix motif in fusion activity
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Author keywords
[No Author keywords available]
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Indexed keywords
CELL MEMBRANES;
CHARACTERIZATION;
FLUORESCENCE;
HYDROPHOBICITY;
PH EFFECTS;
VIRUSES;
LIPID BILAYER;
BIOCHEMISTRY;
DODECYL SULFATE SODIUM;
GLUTAMINE;
GLYCINE;
HYBRID PROTEIN;
ISOLEUCINE;
LEUCINE;
TRYPTOPHAN;
VIRUS HEMAGGLUTININ;
ALPHA HELIX;
AMINO TERMINAL SEQUENCE;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
HYDROPHOBICITY;
INFLUENZA VIRUS;
LIPID BILAYER;
MICELLE;
NONHUMAN;
PH;
POINT MUTATION;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN FUNCTION;
STRUCTURE ANALYSIS;
VIRUS CELL INTERACTION;
AMINO ACID MOTIFS;
AMINO ACID SEQUENCE;
CELL MEMBRANE;
CIRCULAR DICHROISM;
HEMAGGLUTININS;
HYDROGEN-ION CONCENTRATION;
LIPID BILAYERS;
MAGNETIC RESONANCE SPECTROSCOPY;
MICELLES;
MICROSCOPY, FLUORESCENCE;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
ORTHOMYXOVIRIDAE;
PEPTIDES;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT FUSION PROTEINS;
SODIUM DODECYL SULFATE;
SPECTROMETRY, FLUORESCENCE;
SURFACE-ACTIVE AGENTS;
TRYPTOPHAN;
VIRAL PROTEINS;
INFLUENZA VIRUS;
RNA VIRUSES;
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EID: 0037151005
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M200089200 Document Type: Article |
Times cited : (47)
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References (36)
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