Comparison of apoA-I helical structure and stability in discoidal and spherical HDL particles by HX and mass spectrometry

Journal of Lipid Research

Volumn 54, Issue 6, 2013, Pages 1589-1597

  Sevugan Chetty, Palaniappan ^a   Nguyen, David ^a   Nickel, Margaret ^a   Lund Katz, Sissel ^a   Mayne, Leland ^b   Englander, S Walter ^b   Phillips, Michael C ^a  

^a CHILDREN S HOSPITAL OF PHILADELPHIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Amphipathic helix; Cholesterol; Hydrogen exchange; Lipoprotein; Phospholipid

Indexed keywords

APOLIPOPROTEIN A1; DISCOIDAL HIGH DENSITY LIPOPROTEIN; HIGH DENSITY LIPOPROTEIN; SPHERICAL APOLIPOPROTEIN A1; SPHERICAL HIGH DENSITY LIPOPROTEIN; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; ANALYTIC METHOD; ARTICLE; BETA TURN; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HYDROGEN EXCHANGE METHOD; MASS SPECTROMETRY; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; RESIDUE ANALYSIS; STRUCTURE ANALYSIS;

AMPHIPATHIC Α-HELIX; CHOLESTEROL; HYDROGEN EXCHANGE; LIPOPROTEIN; PHOSPHOLIPID;

APOLIPOPROTEIN A-I; HUMANS; LIPOPROTEINS, HDL; MASS SPECTROMETRY; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY;

EID: 84877909378     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M034785     Document Type: Article

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