Figure 3: Propagation of structural perturbations in the M1 mutant.
From: Overlap between folding and functional energy landscapes for adenylate kinase conformational change
Perturbations resulting from the mutation were quantified on the basis of combined absolute 15N and 1H chemical shift differences between WT and mutant, calculated according to δω=0.2 × |Δ15N|+|Δ1H| (p.p.m.)16. As a result of the point mutation, structural rearrangements are propagated throughout the entire ATPlid, with the exception of residues in the INSERT segment (indicated with a dashed oval). (a) Chemical shift differences for non-mutated residues plotted against the primary sequence; threshold values used in (b) are indicated with red and orange lines. (b) Chemical shift perturbations displayed on the open AKe structure (4AKE.pdb); perturbations are colour coded as follows: red δω>0.4 p.p.m., orange 0.4>δω>0.2 p.p.m.; residues that are unassigned in either WT or M1 and proline residues are coloured blue. The mutation site and residues F19, E143 and L178 are shown as dark blue ball and sticks. (c, d) Expansions of 1H-15N HSQC spectra of WT (blue) and M1 (red) AKe. (c) Chemical shift perturbations of L178 and F19 (both 0.27 p.p.m., calculated as stated above); both these residues are accordingly coloured orange in (b). (d) The chemical shift of E143 is identical in the mutant and WT spectra, consistent with identical structures in the INSERT segment.
