Structural differences between apolipoprotein E3 and E4 as measured by 19F NMR

Protein Science

Volumn 19, Issue 1, 2010, Pages 66-74

  Garai, Kanchan ^a   Mustafi, Sourajit M ^a   Baban, Berevan ^a   Frieden, Carl ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

19F tryptophan; apoE monomers; Denaturation; N terminal region; NMR assignments

Indexed keywords

APOLIPOPROTEIN E3; APOLIPOPROTEIN E4; ISOPROTEIN; MONOMER; MUTANT PROTEIN; TRYPTOPHAN; UREA;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; FLUORINE NUCLEAR MAGNETIC RESONANCE; MUTANT; MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STRUCTURE; WILD TYPE;

APOLIPOPROTEIN E3; APOLIPOPROTEIN E4; FLUORINE; MODELS, MOLECULAR; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; UREA;

EID: 75149141497     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.283     Document Type: Article

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