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- W2020463299 abstract "The 'ball-and-chain' model suggests the existence of a negative site which may attract the positively charged inactivation ball to occlude the pore when the channel is in the open state. For Shaker K+ channels, we propose that the state-dependent negative site be tryptophan-435, which becomes negatively charged after receiving an electron from tyrosine-445. The kinetic scheme for the channel's activation-inactivation coupling as derived from the YW-gated model resembles a successful 'scheme 8' proposed by Zagotta and Aldrich. Our model suggests that the final rapid voltage-independent transition to the open state is due to the deprotonation of tyrosine-445." @default.
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- W2020463299 title "On the activation-inactivation coupling in Shaker potassium channels" @default.
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- W2020463299 doi "https://doi.org/10.1016/0014-5793(92)80976-n" @default.
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