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. 2020 Feb 5;253(2):87–99. doi: 10.1007/s00232-020-00108-3

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© The Author(s) 2020

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Fig. 3 — a Interaction of R126 (TM4) with N29 and S68 in TM1 and TM2, respectively. R126H may alter the conformational stability of TM4 and TM2. For R126L mutation, the introduced hydrophobic leucine may interact with another hydrophobic residues or may involve cluster formation via interaction between R126L, I71, and I33. b Modeling of L156, L156R, or L156N. In particular, L156N may cause conformational changes via L156N-S148 side-chain interaction. See Table 1