Structural Determinants of Misfolding in Multidomain Proteins
Fig 5
Free energy profile of WT and its circular permutant domains.
The structures of SH3 and Ubiquitin are shown in (a) and (c), with the “cut” positions K in the WT to form circular permutant labeled with crosses. (b) is the free energy surfaces F(Q) of WT SH3 as well as its circular permutants at 300K. (d) is the F(Q) of WT Ubiquitin and its circular permutants at 290K. The labels K indicate the residue index of the cut position. The free energy curves of the circular permutant cases are shifted vertically for visual clarity, and coloured using the colours corresponding to the crosses in (a) and (c). The free energy plots of the other systems: GB1, SH2, TNfn3 and PDZ are shown in Fig A in S1 Text.