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. 2021 Jan 15;2021:6673661. doi: 10.1155/2021/6673661

Figure 2.

Figure 2

Effect of W196 replacement on the hAIFΔ1-101 ability to stabilize dimers. Elution profile of (a) WT, (b) W196Y, (c) W196L, and (d) W196A on a Sephadex S-200 column at 6°C. The assays were performed in absence and presence of a 10-fold excess of NADH, and profiles are, respectively, shown in black continuous and dashed lines. The respective different populations assigned by Gaussian analysis are depicted in grey lines. (e) Chemical cross-linking of hAIFΔ1-101 samples (~3 μM proteins) with a 100-fold excess of the BS3 cross-linker in the absence and presence of NADH (300 μM). After 45 minutes of incubation, the reactions were stopped by the addition of bromophenol sample buffer and resolved by 12% SDS-PAGE.