Building on previous work (Pless, 2013), we argue that side-chain 'flip out' is a key event in potassium channel C-type inactivation, and propose a new method for encoding multiple noncanonical amino acids and controlling protein stoichiometry.

Type 1 potassium channels alter their composition and localisation to suppress hyper-excitability and neuropathic pain of injured sensory neurons.

The conformation of an isoleucine gate located along the TM6 segment on the intracellular side below the selectivity filter is a critical component leading to a non-conductive state in the C-type inactivation process of K⁺ channels.

The structure of a voltage-activated potassium channel in lipid nanodiscs solved using cryo-electron microscopy is similar to previous X-ray structures, and provides insights into the mechanism of C-type inactivation.

Contrary to a generally accepted principle, the pore properties of KCNQ1 channels depend on the states of voltage-sensing domains activation; KCNE1 alters the voltage-sensing domains-pore coupling to modulate KCNQ1 channel properties.

Tuning the strength of inter- and intra-subunit hydrogen bonds can control potassium flux across biological membranes.

The tarantula toxins psalmotoxin and guangxitoxin have a similar concave surface for interacting with α-helices in voltage-gated and acid-sensing ion channels.

A chain of residues connecting the voltage sensing domain and the pore domain is responsible for a noncanonical communication between these domains.

Structures of the non-canonical potassium channel TMEM175 in open and closed states reveal unique mechanisms for channel gating and the selective permeation of K+ ions.

Charybdotoxin, a toxin produced by scorpions, blocks a K⁺ channel by binding in a lock-and-key fashion to the mouth of the channel and presenting a lysine amino group, which serves as a K⁺ mimic in the selectivity filter.