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. 2017 Dec 5;59(2):348–356. doi: 10.1194/jlr.M080986

Fig. 2.

Fig. 2.

Unfolding of apoA-I in rHDL monitored by the ellipticity at 222 nm. rHDLs were made with WT apoA-I (*), apoA-I[R123A] (open circle), apoA-I[R123E] (open triangle), or apoA-I[R131A] (closed circle). A: Thermal unfolding was induced by heating the proteins from 2°C to 98°C in the cuvette within the CD spectrometer holder. B: Chemical unfolding was induced by incubation of aliquots of rHDL with various concentrations of GndHCl, ranging from 0 to 5 M, at 4°C for 72 h, and then ellipticity at 222 nm was recorded at 25°C.