The structure of human apolipoprotein E2, E3 and E4 in solution: 1. Tertiary and quaternary structure

Biophysical Chemistry

Volumn 119, Issue 2, 2006, Pages 158-169

  Barbier, Anne ^a,b   Clément Collin, Vanessa ^b   Dergunov, Alexander D ^c   Visvikis, Athanase ^a   Siest, Gérard ^a   Aggerbeck, Lawrence P ^b  

^a Centre du Medicament URA CNRS 597   (France)

^b CENTRE DE GÉNÉTIQUE MOLÉCULAIRE   (France)

^c NATIONAL MEDICAL RESEARCH CENTER FOR THERAPY AND PREVENTIVE MEDICINE   (Russian Federation)

Author keywords

Apolipoprotein E; Lipid protein interactions; Lipoprotein; Protein conformation; Receptor binding domain

Indexed keywords

APOLIPOPROTEIN E2; APOLIPOPROTEIN E3; APOLIPOPROTEIN E4; CHYMOTRYPSIN; DIMER; ELASTASE; MONOMER; SUBTILISIN; TETRAMER; TRYPSIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; HUMAN; MATHEMATICAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN LIPID INTERACTION; PROTEIN QUATERNARY STRUCTURE; RECEPTOR BINDING; SEDIMENTATION RATE; STAPHYLOCOCCUS AUREUS;

APOLIPOPROTEIN E2; APOLIPOPROTEIN E3; APOLIPOPROTEIN E4; APOLIPOPROTEINS E; CHEMISTRY, PHYSICAL; CHROMATOGRAPHY, GEL; ENZYMES; HUMANS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SENSITIVITY AND SPECIFICITY; SOLUTIONS;

ESCHERICHIA COLI; STAPHYLOCOCCUS AUREUS;

EID: 30844470880     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2005.07.010     Document Type: Article

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