Thermal transitions in serum amyloid A in solution and on the lipid: Implications for structure and stability of acute-phase HDL

Journal of Lipid Research

Volumn 56, Issue 8, 2015, Pages 1531-1542

  Jayaraman, Shobini ^a   Haupt, Christian ^b   Gursky, Olga ^a  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF ULM   (Germany)

Author keywords

Circular dichroism spectroscopy; Differential scanning calorimetry; Exchangeable apolipoprotein A I; High density lipoprotein; Lipid induced helix folding; Protein lipid interactions; Thermodynamically irreversible transition

Indexed keywords

AMYLOID A PROTEIN; APOLIPOPROTEIN A1; HIGH DENSITY LIPOPROTEIN; 1-PALMITOYL-2-OLEOYLPHOSPHATIDYLCHOLINE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; PHOSPHATIDYLCHOLINE; SERUM AMYLOID A; SOLUTION AND SOLUBILITY;

ALPHA HELIX; AMYLOID A BLOOD LEVEL; ARTICLE; BLOOD LEVEL; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN SECRETION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN UNFOLDING; TEMPERATURE DEPENDENCE; TEMPERATURE RELATED PHENOMENA; THERMAL TRANSITION; WESTERN BLOTTING; ACUTE PHASE RESPONSE; ANIMAL; BLOOD; CHEMISTRY; DRUG EFFECTS; METABOLISM; PROTEIN DENATURATION; SOLUTION AND SOLUBILITY; TEMPERATURE;

ACUTE-PHASE REACTION; ANIMALS; DIMYRISTOYLPHOSPHATIDYLCHOLINE; HUMANS; LIPOPROTEINS, HDL; MICE; PHOSPHATIDYLCHOLINES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; SERUM AMYLOID A PROTEIN; SOLUTIONS; TEMPERATURE;

EID: 84941282386     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M059162     Document Type: Article

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