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. Author manuscript; available in PMC: 2018 Jan 10.
Published in final edited form as: J Mol Biol. 2017 May 20;429(14):2192–2210. doi: 10.1016/j.jmb.2017.05.015

Figure 4.

Figure 4

H37 chemical shifts in WT (a) and W41F (b, c) AM2-TM from 2D 13C-13C (a, b) and 15N-13C (c) correlation spectra as a function of pH. (a) H37 Cα-Cβ regions of the 2D 13C-13C spectra of the WT peptide. (b) H37 Cα-Cβ and aliphatic-aromatic regions of the 2D 13C-13C spectra of the W41F mutant. (c) Aromatic region of the 2D 15N-13C correlation spectra of the W41F mutant. The pH and drug binding state of the samples are indicated. The mutant channel shows higher π tautomer intensities at high pH and more cationic histidine peaks at low pH compared to the WT channel.