Fig. 1
From: A post-translational modification of human Norovirus capsid protein attenuates glycan binding
Exchange of backbone NH protons and protein concentration affect spectral quality. a 1H,15N TROSY HSQC spectra of 100 µM [U-2H,15N] labeled GII.4 Saga P-dimers before (black) and after (red) protein refolding recorded on a Bruker AVIII 500 MHz NMR spectrometer. Samples were prepared in buffer containing 75 mM sodium phosphate, 100 mM NaCl, and 100 µM DSS-d6 in 10% D2O with the pH* adjusted to 7.30 and with the temperature set at 298 K. b Non-exchangeable NH protons (red color) mapped onto the surface of GII.4 Saga P-dimers (pdb: 4X06). c Positive 1H-15N projection of all planes along the 13C dimension of 3D TROSY HN(CO)CACB spectra acquired under identical conditions (in sodium phosphate 20 mM, pH* 7.30) for [U-2H,13C,15N] GII.4 Saga P-dimers at concentrations of 180 µM (left) and of 300 µM (right). Source data are provided as a Source Data file
