Figure 2 | Scientific Reports

Figure 2

From: The de novo design of a biocompatible and functional integral membrane protein using minimal sequence complexity

Figure 2

Affinity purification and characterization of REAMP. (a) Representative SDS-PAGE gel showing cell fractionation and purification of REAMP in Cymal-5. Immunodetection with anti-V5 (IB α-V5) confirms the protein identity and the success of the purification strategy. The uncropped blot is shown as Fig. S7. (b) Size exclusion chromatography shows that purified REAMP is homogenous and monodisperse in Cymal-5 with an apparent molecular weight of 65 kDa. SDS-PAGE analysis confirms that the peak is REAMP. The uncropped gel is presented as Fig. S8. (c) Purification of REAMP in other maltosides suggests that the protein contribution to the PDC is 43 ± 9 kDa, consistent with three protomers per micelle. Data are from SEC profiles shown in Fig. S9. (d) The PDC is apparently 60 kDa on blue native PAGE.

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