Extended Data Fig. 6: Circular dichroism analysis of the interactions of proteins with SNPs in the absence or presence of cholesterol.
(a-h) Circular dichroism (a, c, e, g) and secondary structure (b, d, f, h) of APOE (a-b), C1Q (c-d), LDL (e-f) and HDL (h-g) in the absence and presence of cholesterol or SNPs. The conformation of APOE and C1Q changed after interacting with SNPs. Even though cholesterol itself did not induce conformational changes, it further enhanced the conformational change of APOE elicited by SNPs. The conformation of LDL and HDL could be altered by both cholesterol and SNPs, and the change became more distinct in the presence of both cholesterol and SNPs.
