PMC

X-ray crystal structure of S. cerevisiae eEF1A (shading) shows that the SBD mutations (arrows) T22 (S, magenta), A112 (T, cyan), A117 (V, T, purple), E122 (K, yellow), D156 (E, N, orange), and R164 (K, pink) that suppress the requirement for the eEF1Bα (brown) cluster in the GTP-binding domain (Andersen et al. 2000). GDP is shown in green.

Selected site-resolved measurements of transverse relaxation rate constants, R_1ρ and R₂, for residues in the amyloid core region of huPrP23-144 fibrils. ¹H^N R_1ρ (A) and ¹⁵N R₂ (B) trajectories, recorded using pulse schemes in Figure S3, are shown for residues A117, L130 and S132. Best-fit simulations to decaying single exponential curves are shown as solid lines. Additional ¹H^N R_1ρ, ¹³C^α R_1ρ, ¹⁵N R_1ρ and ¹⁵N R₂ trajectories are shown in Figures S8-S11.

XPV mutations. a. R111 contacts DNA template and stacks with P316 of LF. b. Mapping of 8 missense XPV mutations. The protein is represented by the Cα trace, DNA as tube-and-ladders, and the altered residues are shown as cyan ball-and-sticks. c. Local interactions of A117 and T122 and their relation to the active site. Most side chains are removed for clarity. d. R361 supports P316 and the β strand that forms an extensive hydrogen-bond network with the DNA template. e. G263 and A264 are adjacent to the thumb-DNA primer interface. G263V and A264P substitutions would clash with L258 and K261. Electron densities are shown as meshes in panels c and e.

Time evolution of the total SASA (A) and corresponding free energy profile, ΔA, as a function of the total SASA (B) for the oligomeric simulation of the WT and A117V mutant peptides. Representative β-sheet oligomeric structures are also given. (C) Distribution of the number of intrapeptide and interpeptide hydrogen bonds in the simulation of the oligomeric WT and A117V mutant peptides. (D) Distribution of the SASA fraction of the side chain of residue A117 (for the WT) and V117 (for the mutant) in the simulation of the oligomeric WT and A117V mutant peptides. The fraction is given with respect to the corresponding SASA in the starting configuration.