Fig. 4
From: Conformational dynamics in the disordered region of human CPEB3 linked to memory consolidation
Conformation of the NES and nearby putative phosphoTyr site. A (Top) Residues L346-L349 and S352-M356 adopt two short, partially populated α-helices. (Bottom). Representative conformer is shown with cationic residues (R and K) colored blue, aromatics (F, Y, and H) = purple, anionic (E and D) = red, aliphatic (I, L, M) = dark gray, amyloidogenic (N and Q) = magenta, hydroxyl bearing (S and T) = cyan, and proline = green. Spiral ribbons mark the helical segments spanning residues 346–349 and 352–356. B Conformational chemical shifts of 13Cα (blue bars) and 13CO (black narrow bars) afford detection of helical conformations. Uncertainties in the conformational chemical shifts (Δδ) are 0.02 and 0.10 ppm for 13CO and 13Cα, respectively. C {1H}-15 N NOE ratios of 0.85 and − 0.20 are indicative of high rigidity and flexibility, respectively, on ps-ns time scales. D Higher R1ρ rates are diagnostic of rigidity on µs-ms time scales