Fig. 5: Omp2a folding with tES–F116H.
From: A general approach to protein folding using thermostable exoshells
a tES–F116H(+) encapsulates a single monomer of Omp2a (b) Omp2a monomers released from tES–F116H(+) form trimeric assemblies after a nine-day incubation period. c, d, e SEC demonstrates complete trimerization only in the setting of tES116H(+)-mediated folding. f AUC demonstrates that the ability to form Omp2a trimers is affected by tES–F116H internal charge. Omp2a folded without tES–F116H does not demonstrate trimerization. g Intrinsic fluorescence of Omp2a refolded and released from tES(+)F116H, tES(+/–)F116H, and tES(–)F116H, and Omp2a refolded without tES. (Data are presented as mean ± SEM., n = 3 independent experiments). h Conductance measurements of the 172-kDa Omp2a trimeric SEC fraction demonstrate a range of 1–4 nS. i A positive control of Omp2a demonstrates similar conductance insertions (Source data are provided as a Source Data file).
