Fig. 2: Screening of various constructs indicated that the POTRA domain of Oep80 causes aggregation whereas the β-barrel domain alone can produce a monodisperse SEC peak. | Communications Biology

Fig. 2: Screening of various constructs indicated that the POTRA domain of Oep80 causes aggregation whereas the β-barrel domain alone can produce a monodisperse SEC peak.

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

Fig. 2

a AlphaFold predicted structure of mature Oep8035. The cleavable transit peptide has been removed. b Domains of full-length AtOep80 (1.), plus constructs of Oep80 used to screen for refolding from E. coli inclusion bodies: 2 = 6×His-Oep80, 3 = 6×His-Oep80POTRA, 4 = Oep80β-6×His. c Overlaid SEC traces of different Oep80 constructs. TP= chloroplast transit peptide, Dis.=disordered region, P = POTRA domain, β = β-barrel domain. N and C refer to the N- and C-termini, respectively.

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