Figure 2. Lipid binding property of the Δ191–220 apoA-I variant.
(A) Binding isotherms of wild-type (●) and Δ191–220 (○) apoA-I to egg PC SUV. (B) Far-UV CD spectra of wild-type (solid line) and Δ191–220 (dotted line) apoA-I in the presence of SUV. Correlation of the enthalpy (C) and the free energy (D) of binding of apoA-I variants with the increase in α-helix content upon binding to egg PC SUV. Data of deletion variants and human apoA-I (plasma) are added from [21].
