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. 2019 Oct 31;10:4972. doi: 10.1038/s41467-019-12865-4

Fig. 4.

Fig. 4

TM3 and TM4 in nhTMEM16 are locked in hydrophobic interactions mediated by the L302/I343/L347 triad of residues. a Two views, related by 90 rotation around the membrane normal, of the groove region in the WT nhTMEM16 protein, show the locations of L302, I343, and L347 (in space fill and labeled). Helices TM3-TM6 that line the groove are labeled, and colored red, blue, white and gray, respectively. b Histograms of minimal distance between residue pairs L302 and I343 (in red), and L302 and L347 (in black), in the simulation trajectories of WT nhTMEM16 (see also Supplementary Fig. 6)