Fig. 4: Alkaline phosphatase folding with tES–F116H.
From: A general approach to protein folding using thermostable exoshells
a Release of sAP from tES–F116H charge variants results in a dimeric peak for tES–F116H(+) and tES–F116H(+/–), however, monomeric sAP was observed with sAP folded alone [sAP(a)] and aggregation was seen with the use of tES-F116H(–). b, c Titration of Zn and Mg yields activity increases similar for caged versus released sAP and a solubly expressed sAP control. d, e Titration of Zn and Mg has differential effects on sAP intrinsic fluorescence, a marker of folding. f AUC of tES-F116H(+) loaded with sAP demonstrates a M.W. of 522 kDa, consistent with encapsulation of a single sAP monomer. g Activity of sAP is moderately increased after release from three charge variants of tES–F116H. h Intrinsic fluorescence is optimal when sAP is folded with charge-matched tES–F116H(+). (b, c, d, e, g, h, data are presented as mean ± SEM., n = 3 independent experiments) (Source data are provided as a Source Data file).
