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• W1996936601 abstract "We used molecular dynamics (MD) simulations to explore the transport of single cations through the channel of the muscle nicotinic acetylcholine receptor (nAChR). Four MD simulations of 16 ns were performed at physiological and hyperpolarized membrane potentials, with and without restraints of the structure, but all without bound agonist. With the structure unrestrained and a potential of −100 mV, one cation traversed the channel during a transient period of channel hydration; at −200 mV, the channel was continuously hydrated and two cations traversed the channel. With the structure restrained, however, cations did not traverse the channel at either membrane potential, even though the channel was continuously hydrated. The overall results show that cation selective transport through the nAChR channel is governed by electrostatic interactions to achieve charge selectivity, but ion translocation relies on channel hydration, facilitated by a trans-membrane field, coupled with dynamic fluctuations of the channel structure." @default.
• W1996936601 created "2016-06-24" @default.
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• W1996936601 date "2008-02-15" @default.
• W1996936601 modified "2023-09-25" @default.
• W1996936601 title "Control of Cation Permeation through the Nicotinic Receptor Channel" @default.
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• W1996936601 doi "https://doi.org/10.1371/journal.pcbi.0040041" @default.
• W1996936601 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2242826" @default.
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