Figure 5
A comparison of μs-ms timescale conformational exchanges between HuPrP(G127V) and WT HuPrP. All CPMG RD experiments were conducted at magnetic field strengths of 14.10 T (red for G127V, violet for WT) and 19.97 T (blue for G127V, olive for WT). The individual interconversion rates (kex) were mapped onto the 3D structures of the mutant and WT proteins. Gly131, Tyr163, Gln172 and Gln186 in the mutant are coloured light blue, TextView blue, blue and marine, respectively. Gln172 and Ile182 from the WT protein are coloured smudge and chartreuse, respectively. The colours of the spheres on the 3D structures show the changing tendency from bright to dark, corresponding to the declining tendency of kex for the related residues.
