Fig. 5: Effects of truncation of the OmpX-derived QMN (b2) peptide on the methyl-TROSY NMR spectrum of SurA-WT.
From: Dual client binding sites in the ATP-independent chaperone SurA
Intensity ratio (a, c) and CSP (b, d) plots are shown for SurA-WT bound to (a, b) the N-terminal 8 residues of QMN (QMNN-term - QMNKMGGF), and (c, d) the C-terminal 7 residues of QMN (QMNC-term - NLKYRYE). Peaks which were broadened beyond detection in peptide-containing samples are indicated with an asterisk. Conf.: residues indicative of conformational change (Supplementary Fig. 14). Samples contained 5 µM SurA ± 200 µM peptide, 5 mM EDTA, 20 mM Tris-HCl, pH 8, at 25 °C. int: intensity. Signal to noise ratios were used for the calculation of errors in peak intensities in (a, c) (Methods). Source data are provided as a Source Data file.
