Figure 7. R_hcomparisons to number of residuesNfor folded and intrinsically disordered proteins.

This set was limited to N > 50 and used R_h from published reports (26,32,54,63–81). In panel A, the line labeled “coil” shows R_h calculated using equations 1 and 2 with S_PPII = 0. Filled circles are IDPs and open circles are folded proteins. In panel B R_h values for IDPs were converted to RSC_PPII RSC_PPII was determined for each IDP by first calculating the statistical coil ∂R_h/∂f_PPII (which varies with N) and IDP ∂R_h/∂f_PPII using the method given in Figure 1 for wild type p53(1–93). These two ∂R_h/∂f_PPII values were then divided (IDP/coil) to give RSC_PPII. For p53(1–93), the averaged R_h (32.4 Å) was used to determine RSC_PPII rather than the DLS-measured R_h (32.8 Å). The dashed line shows the averaged RSC_PPII (2.3 ± 0.8) from the set of IDPs in panel A.