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

Biochemistry

Volumn 48, Issue 2, 2009, Pages 289-301

  Qiang, Wei ^a   Weliky, David P ^a  

^a MICHIGAN STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR MEMBRANES; CO GROUPS; EFFICIENT SYNTHESIS; ENVELOPE PROTEINS; ENVELOPED VIRUS; FUSION ACTIVITIES; FUSION PEPTIDES; HEAD GROUPS; HIGH-YIELD SYNTHESIS; MEMBRANE CHOLESTEROLS; MEMBRANE VESICLES; MODEL SYSTEMS; N TERMINALS; SOLID-STATE NMR; STRAND CONFORMATIONS; TETRAMER; VESICLE FUSIONS;

AMINES; CELL MEMBRANES; CHEMICAL SHIFT; CHOLESTEROL; CROSSLINKING; CYTOLOGY; INTERNET; MEMBRANES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERS; POLYMERS; SYNTHESIS (CHEMICAL); VIRUSES;

CONFORMATIONS;

ALANINE; CHOLESTEROL; DIMER; HUMAN IMMUNODEFICIENCY VIRUS PROTEIN; HYBRID PROTEIN; LIPID; MONOMER; OLIGOMER; PHOSPHORUS 31; TETRAMER; VIRUS ENVELOPE PROTEIN; CROSS LINKING REAGENT; GLYCOPROTEIN GP 41; PEPTIDE;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CATALYSIS; CELL MEMBRANE; CROSS LINKING; HUMAN IMMUNODEFICIENCY VIRUS; MEMBRANE FUSION; MEMBRANE VESICLE; MOLECULAR SIZE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN LIPID INTERACTION; PROTEIN SYNTHESIS; PROTON NUCLEAR MAGNETIC RESONANCE; TARGET CELL; AMINO ACID SEQUENCE; CHEMISTRY; COMPUTER SIMULATION; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SYNTHESIS; TEMPERATURE;

AMINO ACID SEQUENCE; CELL MEMBRANE; CHOLESTEROL; COMPUTER SIMULATION; CROSS-LINKING REAGENTS; HIV; HIV ENVELOPE PROTEIN GP41; KINETICS; LIPIDS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE;

EID: 59849106607     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8015668     Document Type: Article

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