In the Multi-domain Protein Adenylate Kinase, Domain Insertion Facilitates Cooperative Folding while Accommodating Function at Domain Interfaces
Figure 5
Folding of AKE mutants with deleted inter-domain interfaces.
All free energies are scaled by their respective kBTfs. N and U denote the native and the unfolded ensembles. The error bars represent twice the square root of the variance in the folding free energy and were calculated using a jackknife algorithm. The blue Xs mark the position of the deleted interfaces. (A) Cartoon of the folded state of ΔCORE-NMPi at Tf. (B) The FEP (black with blue error bars) shows a free energy barrier similar to that in WT (grey). (C) Q* and Q*NMP are strength-scaled fraction of native contacts, e.g., a contact with a strength of 1.2 is counted as 1.2, when formed, in the calculation of Q* and Q*NMP. The 2DFES plot with RCs of Q*NMP and Q* shows that NMP folds as in WT. (D) Cartoon of the folded state of ΔCORE-LIDi at Tf. (E) The FEP (black with blue error bars) shows a free energy barrier similar to that in WT (grey). The U ensemble shifts to higher Q*. (F) The 2DFES plot with RCs of Q*LID and Q* shows that the U ensemble has partially folded LID.