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. 2017 Sep 1;114(38):E7977–E7986. doi: 10.1073/pnas.1704640114

Fig. 6.

Fig. 6.

The prodomain is intrinsically disordered. (A) An electrostatic potential map of the procaspase-6 prodomain with its corresponding amino acid sequence. The blue and red regions represent the relative localization of the positive and negative potentials, respectively. (B) The deuterium uptake profile of a representative peptic peptide (2–19) in the prodomain identified in the prodomain-containing caspase-6 maturation variants. The asterisk designates the D to A substitution at the indicated proteolytic cleavage site, rendering that site uncleavable. Error, SD of duplicate H/DX-MS measurements done on 2 separate days. (C) The corresponding MS spectra of peptide 2–19 presented in B. (D) Prediction of the disordered (blue) and protein-binding (orange) regions of caspase-6 using DISOPRED server. (E) CD spectra of cleaved caspase-6 with (D23A D179CT) and without (ΔN D179CT) the prodomain.