Fig. 2.

R95G p97-ADP disease mutant is plastic. (A) ¹³C-¹H multiple quantum relaxation dispersion profiles (50 °C, 18.8T) for selected residues in the NTD (I16, I119), NTD–D1 linker (I189, L213), and the D1 domain (L229, I274) for R95G ND1Lp97-ADP (blue) and the corresponding molecule with the NTD domain covalently tethered to D1 (black). A global fit is included for the R95G profiles based on an analysis of 22 residues (Combined Fits of Chemical Shift and CPMG Data). (B) Three-state exchange model that takes into account both the ¹³C chemical shift data (Fig. 1B) and CPMG dispersion data that consists of the NTD up (U)/down (D) equilibrium and an additional process involving a third state, C. Reduced χ² surfaces for rates for the first and second processes for the R95G mutant. (C) Positions of methyl groups from which CPMG dispersion profiles were analyzed via a global fit of the data using the model in B. Methyls are shown as spheres on the X-ray structure of ND1Lp97-ADP color-coded by the size of differences between ¹³C chemical shifts measured in spectra of R95G ND1Lp97-ADP and for the corresponding probes in state C (Combined Fits of Chemical Shift and CPMG Data), |Δϖ|. (D) Histogram of fitted $R_2^{\infty }$ rates for R95G ND1Lp97-ADP.