In voltage-gated Na+ and K+ channels, the hydrophobicity of non-charged residues in the
S4 helix has been shown to regulate the S4 movement underlying the process of voltage …

The voltage-gated proton channel H v 1 is a member of voltage-gated ion channels
containing voltage-sensing domains (VSDs). The VSDs are made of four membrane …

Part of the “signature sequence” that defines the voltage-gated proton channel (HV1) is a
tryptophan residue adjacent to the second Arg in the S4 transmembrane helix: RxWRxxR …

The voltage sensor domain (VSD) is the key module for voltage sensing in voltage-gated ion
channels and voltage-sensing phosphatases. Structurally, both the VSD and the recently …

ATP is an important molecule implicated in diverse biochemical processes, including the
modulation of ion channel and transporter activity. The voltage‐gated proton channel (Hv1) …

The voltage-gated proton channel Hv1 has a voltage sensor domain but lacks a pore
domain. Although the C-terminal domain of Hv1 is known to be responsible for dimeric …

Voltage-gated sodium, potassium, and calcium channels are made of a pore domain (PD)
controlled by four voltage-sensing domains (VSDs). The PD contains the ion permeation …

Voltage‐gated proton (Hv) channels have long been found with electrophysiological tools in
many different cell types. However, the molecular identity of Hv channels was not discovered …

Voltage‐gated proton channels have been described in different cells and organisms since
the early'80s, but the first member of the family, Hv1, was cloned only recently. The Hv1 …

In voltage-gated sodium, potassium and calcium channels, the functions of ion conduction
and voltage sensing are performed by two distinct structural units: the pore domain and the …