Abstract
Connexins (Cxs) are a family of integral membrane proteins gated by numerous conditions. A recent cryo-EM investigation of Cx26 gap junctional channel revealed an open and a closed conformations co-exist at pH 6.4. This result suggests that the protonation state of histidine residues govern the conformational dynamics of Cx26, especially at N-terminal and cytoplasmic loop regions. To explore the molecular mechanism of pH-gating of Cx26, all-atom molecular dynamics simulations and constant pH simulations are employed.
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