Fig. 3: The engineered perfectly repetitive sequence, prf.GLFG_52 × 12 improves the resolution of NMR measurements.

a Overlay of ¹⁵N-¹H correlation spectra (¹⁵N-¹H HSQC^SSMAS) of phase-separated Mac98A FG domain (forest green) and prf.GLFG_52 × 12 (light green), where each peak corresponds to an amide group with a distinct chemical environment. b ¹⁵N-¹H HSQC^SSMAS of prf.GLFG_52 × 12 (purple) and the TROSY spectrum (red). The peak positions are shifted by half the ¹J(¹⁵N,¹H) coupling in both dimensions as expected. Assignments of the prf.GLFG_52 × 12 are shown beside the peaks (also see Supplementary Fig. 4). Proline residues lack H^N, and thus are not detected. c ¹³C-¹H HSQC^SSMAS spectrum of prf.GLFG_52 × 12. The cross peaks corresponding to CH bonds of the Phe aromatic sidechain are enlarged and labelled with their relative intensities (2:2:1).