Alpha-helix formation is required for high affinity binding of human apolipoprotein A-I to lipids

Apolipoprotein (apo) A-I is thought to undergo a conformational change during lipid association that results in the transition of random coil to alpha-helix. Using a series of deletion mutants lacking different regions along the molecule, we examined the contribution of alpha-helix formation in apoA...

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Veröffentlicht in:	The Journal of biological chemistry 2004-05, Vol.279 (20), p.20974-20981
Hauptverfasser:	Saito, Hiroyuki, Dhanasekaran, Padmaja, Nguyen, David, Deridder, Els, Holvoet, Paul, Lund-Katz, Sissel, Phillips, Michael C
Format:	Artikel
Sprache:	eng
Schlagworte:	Apolipoprotein A-I - metabolism Chromatography, Gel Circular Dichroism Humans Liposomes - metabolism Phosphatidylcholines - metabolism Protein Structure, Secondary Spectrophotometry, Ultraviolet
Online-Zugang:	Volltext
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