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. Author manuscript; available in PMC: 2016 Jun 16.
Published in final edited form as: Nature. 2015 Dec 16;528(7583):580–584. doi: 10.1038/nature16162

Extended Data Figure 7. Designs are stable to chemical denaturation by guanidine HCl (GuHCl).

Extended Data Figure 7

Circular dichroism monitored GuHCl denaturant experiments were carried for two designs for which crystal structures were solved (DHR4 and DHR14), two with overall shapes confirmed by SAXS (DHR21 and DHR62), and two with overall shapes inconsistent with SAXS (DHR17 and DHR67). In contrast to almost all native proteins, four of the six proteins do not denature at GuHCl concentrations up to 7.5 M. Both designs not confirmed by SAXS were extremely stable to GuHCl denaturation and hence are very well folded proteins; the discrepancies between the computed and experimental SAXS profiles may be due to small amounts of oligomeric species or variation in overall twist.