Fig. 1: NMR evidence for the engagement of residue Gly22 of E22G-Aβ40 in an NH-π interaction.
From: Direct detection of an NH-π hydrogen bond in an intrinsically disordered peptide
a Amino acid sequence of wild-type (WT) and E22G-Aβ40 in single letter code, with the mutation site and fluorinated amino acids highlighted by a dashed box and bold fonts, respectively. b 15N,1H HSQC spectra of E22G-Aβ40 measured at temperatures 278–298 K, showing the remarkable lack of temperature sensitivity for the N and HN chemical shifts of Gly22, while the other six glycines exhibited large temperature sensitivity typical of unstructured proteins. c Residue-specific temperature coefficients of HN chemical shifts for the WT and E22G-Aβ40. Residue Gly22 shows a near-zero temperature coefficient in the E22G-Aβ40 peptide. d Schematic representation of the suggested hydrogen bond between the amide proton of Gly22 and the aromatic side chain of Phe20 lying roughly beneath it (the cartoon of the peptide backbone created in BioRender. Russo, L. (2025) https://BioRender.com/jct0ak3).
