Figure 2
SRCD spectroscopy determines concentration and lipid-state dependent secondary structure distribution in apoA-I WT, Milano and A164S proteins. (a) Soluble proteins (McIlvaine Buffer) were scanned by SRCD spectroscopy (in the range of 190–260 nm) at indicated protein concentrations (0.1 mg/ml, 0.5 mg/ml and 1.5 mg/ml for lipid-free (LF) proteins, and 0.5 mg/ml for lipid-bound (LB) protein in 9.6 nm HDL particles). (b,c) The obtained spectra were used for determination of the relative secondary structure distribution (alpha helix, beta strand, turns and unordered) of the proteins. Graphs are shown to either highlight the inter-variant similarities/differences at a given protein concentration and lipidation-state (b), or to visualize the intra-variant protein concentration and lipid-state dependent secondary structure distribution (c). Data is shown as mean ± SD; significance is calculated according to two-way ANOVA (* p < 0.05, **p < 0.005, ***p < 0.001, ****p < 0.0001).
