Fig. 3: Refolded Oep80β behaves as a folded β-barrel protein and exists as a non-hybrid barrel dimer in solution. | Communications Biology

Fig. 3: Refolded Oep80β behaves as a folded β-barrel protein and exists as a non-hybrid barrel dimer in solution.

From: Biochemical characterisation supports a central role for Oep80 from Arabidopsis thaliana in chloroplastic β-barrel protein assembly

Fig. 3

a Overlaid traces from SEC performed on Oep80β refolded using three different detergents. b CD spectrum performed on Oep80β in LDAO. c Native mass spectrum of Oep80β-6×His. For predicted and observed masses, see Supplementary Table 2. d Schematic to show a cross-gate disulfide should prevent hybrid barrel formation. Red circles represent introduced cysteine residues and yellow represents disulfide crosslinking. e AlphaFold 3 model of Oep80β C587S/S408C/G727C, showing a lateral gate-spanning disulfide bond in yellow. Introduced β1 and β-1 cysteines coloured in red. pTM = 0.84. f SDS-PAGE on Oep80β C587S/S408C/G727C post SEC purification and after incubation at 4 °C with 0.1 mM CuSO4 for 3 h. +DTT indicates the sample was boiled with 50 mM DTT in loading dye.

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