Figure 3 | Scientific Reports

Figure 3

From: Specific domain V reduction of beta-2-glycoprotein I induces protein flexibility and alters pathogenic antibody binding

Figure 3

AFM imaging of β2GPI. Untreated (A) and reduced (B) β2GPI with examples of particle structure highlighted. (C) Surface models of β2GPI in the suggested conformation of the structures highlighted in (A) and (B). (D) Distribution of aspect ratios R with the minimum and maximum values (whiskers) plotted with the median, this includes three independent replicates of reduced β2GPI and two replicates (with two technical replicates) of untreated β2GPI. In total, 351 and 352 molecules were analysed, respectively. A higher mean aspect ratio for reduced β2GPI (2.97) compared to untreated β2GPI (2.58) and a significantly increased percentage of open particles (35% vs 25%) were found (p = 0.0003). This suggests that reduction allows β2GPI to be more flexible, which is best reflected as a wider upper distribution of structures with more structures falling above an aspect ratio of 5 (10.5% vs 6.3% reduced and untreated, respectively).

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