Computational study of the transmembrane domain of the acetylcholine receptor |
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Authors: | Chen Song Ben Corry |
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Institution: | (1) School of Biomedical, Biomolecular and Chemical Sciences, The University of Western Australia, Crawley, WA, 6009, Australia |
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Abstract: | The nicotinic acetylcholine receptor (nAChR) is a ligand-gated ion channel protein whose transmembrane domain (TM-domain)
is believed to be responsible for channel gating via a hydrophobic effect. In this work, we perform molecular dynamics and
Brownian dynamics simulations to investigate the effect of transmembrane potential on the conformation and water occupancy
of TM-domain, and the resulting ion permeation events. The results show that the behavior of the hydrophobic gate is voltage-dependent.
Large hyperpolarized membrane potential can change the conformation of TM-domain and water occupancy in this region, which
may enable ion conduction. An electrostatic gating mechanism is also proposed from our simulations, which seems to play a
role in addition to the well-known hydrophobic effect. |
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Keywords: | Ion channel Acetylcholine receptor Gating Membrane potential Molecular dynamics Brownian dynamics |
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