Skip to main content
. Author manuscript; available in PMC: 2022 Jan 4.
Published in final edited form as: Angew Chem Int Ed Engl. 2020 Oct 29;60(1):166–170. doi: 10.1002/anie.202008804

Figure 1.

Figure 1.

Solution NMR study of MPER in H2O. (A) Amino acid sequence of the MPER (residues L660-N674) peptide used in this study, including an N-terminal acetylated Gly and five C-terminal Lys residues. (B) Overlay of the 1H-15N HSQC spectra of 14 mM (green), 3 mM (red) and 1.1 mM (blue) MPER. Assignments are marked for the 1.1 mM sample. (C) Changes in 1H and 15N chemical shifts when increasing MPER concentration from 1.1 mM to 3 mM (red), and from 1.1 mM to 14 mM (green). Spectra were collected at 600 MHz in 50 mM MES buffer, pH 6, 40 °C. The C-terminal poly-Lys residues are shown on a grey background.