Synthetic fusion peptides of tick-borne encephalitis virus as models for membrane fusion

Biochemistry

Volumn 49, Issue 2, 2010, Pages 287-296

  Pan, Jinhe ^a   Lai, C Benjamin ^a   Scott, Walter R P ^a   Straus, Suzana K ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PH; ACYL CHAIN; C-TERMINUS; CIRCULAR DICHROISM; ENVELOPE PROTEINS; FUSION MECHANISM; FUSION PEPTIDES; FUSION PROCESS; HOST CELLS; MEMBRANE FUSION; MOLECULAR DYNAMICS SIMULATIONS; SECONDARY STRUCTURES; SHORT SEGMENTS; SIDE CHAINS; STRAND CONFORMATION; STRUCTURAL STUDIES; TRYPTOPHAN FLUORESCENCE; WILD TYPES;

AMINO ACIDS; CELL MEMBRANES; CYTOLOGY; DICHROISM; MOLECULAR DYNAMICS; MONOMERS; PEPTIDES; PHOTON CORRELATION SPECTROSCOPY; VIRUSES;

PH EFFECTS;

1 PALMITOYL 2 OLEOYL SN GLYCERO 3 PHOSPHOCHOLINE; 1 PALMITOYL 2 OLEOYL SN GLYCERO 3 PHOSPHOETHANOLAMINE; CHOLESTEROL; E PROTEIN; LEUCINE; LIPID; LYSINE; MONOMER; MUTANT PROTEIN; PHOSPHOETHANOLAMINE; PHOSPHORYLCHOLINE; PROTEIN DERIVATIVE; SYNTHETIC PEPTIDE; TRYPTOPHAN; UNCLASSIFIED DRUG; MEMBRANE FUSION PROTEIN; PEPTIDE; PEPTIDE FRAGMENT; VIRUS PROTEIN;

ARTICLE; CIRCULAR DICHROISM; CONFORMATION; CONTROLLED STUDY; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; MEMBRANE FUSION; MOLECULAR DYNAMICS; MUTATION; NONHUMAN; PEPTIDE SYNTHESIS; PH; PHOTON CORRELATION SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SIMULATION; TICK BORNE ENCEPHALITIS FLAVIVIRUS; WILD TYPE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; KINETICS; MOLECULAR GENETICS; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; VIRUS ENTRY;

TICK-BORNE ENCEPHALITIS VIRUS;

AMINO ACID SEQUENCE; COMPUTER SIMULATION; ENCEPHALITIS VIRUSES, TICK-BORNE; KINETICS; MEMBRANE FUSION PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PEPTIDES; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TRYPTOPHAN; VIRAL PROTEINS; VIRUS INTERNALIZATION;

EID: 75349091705     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9017895     Document Type: Article

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