Extended Data Fig. 1: Two-dimensional 1H-15N transverse relaxation optimized spectroscopy (TROSY) spectra of 15N-PTH(1–34).
From: Allosteric interactions in the parathyroid hormone GPCR–arrestin complex formation
Spectra were obtained in the absence (blue) or presence of PTHRECD, 0.5 (pink) or 0.75 (purple) molar ratio. a, On the left panel, full spectra showing all peaks of PTH(1–34). On the right panel, spectra of Gly12 and Ser17. Ser17 peak was too weak to be seen at 0.75 molar ratio. b, Zoomed-in spectra showing most peaks of PTH(1–34). PTH(1–34) peaks are labeled with bold text, and peaks corresponding to attached Strep-tag are labeled with italicized text. c, Zoomed-in spectral region of PTH His9. The conformation of His9 in free PTH is marked by Peak #1. Peak #2 represents the new conformation of His9 that occurred in the presence of 0.5 molar ratio PTHRECD and becomes stronger at 0.75 molar ratio PTHRECD. d, Zoomed-in spectral region of PTH Asn16, showing PTH conformational changes in the presence of PTHRECD. Peak #1 represents the conformation of Asn16 in the free PTH. Peak #2 represents the new conformation of Asn16 when PTH is bound to PTHRECD.
