Apolipoprotein E4 forms a molten globule: A potential basis for its association with disease

Journal of Biological Chemistry

Volumn 277, Issue 52, 2002, Pages 50380-50385

  Morrow, Julie A ^a,b   Hatters, Danny M ^a,b   Lu, Bin ^a,b   Höchtl, Peter ^c   Oberg, Keith A ^d   Rupp, Bernhard ^c   Weisgraber, Karl H ^a,b  

^a GLADSTONE INSTITUTE OF CARDIOVASCULAR DISEASE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c LAWRENCE LIVERMORE NATIONAL LABORATORY   (United States)

^d Allecure Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DISEASES; FOURIER TRANSFORMS; INFRARED SPECTROSCOPY; LIGHT SCATTERING; MOLTEN MATERIALS; PH EFFECTS; UREA;

GLOBULES; ISOFORMS;

PROTEINS;

APOLIPOPROTEIN E2; APOLIPOPROTEIN E3; APOLIPOPROTEIN E4; ISOPROTEIN; PEPSIN A; UREA;

AMINO TERMINAL SEQUENCE; ARTICLE; HYDROPHOBICITY; INFRARED SPECTROSCOPY; LIGHT SCATTERING; MOLECULAR WEIGHT; PH; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION;

APOLIPOPROTEIN E3; APOLIPOPROTEIN E4; APOLIPOPROTEINS E; DIMYRISTOYLPHOSPHATIDYLCHOLINE; HUMANS; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; PEPSIN A; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN ISOFORMS; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; UREA;

EID: 0037184994     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M204898200     Document Type: Article

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