AbstractThe activation of Shaker K+ channels is steeply voltage dependent. To determine whether conserved charged amino acids in putative transmembrane segments S2, S3, and S4 contribute to the gating charge of the channel, the total gating charge movement per channel was measured in channels containing neutralization mutations. Of eight residues tested, four contributed significantly to the gating charge: E293, an acidic residue in S2, and R365, R368, and R371, three basic residues in the S4 segment. The results indicate that these residues are a major component of the voltage sensor. Furthermore, the S4 segment is not solely resposible for gating charge movement in Shaker K+ channels
AbstractIn voltage-dependent ion channels, pore opening is initiated by electrically driven movement...
The S4 transmembraneα-helix in voltage-gated channels contains several regularly spaced basic amino ...
ABSTRACT The cytoplasmic ends of the four S6 transmembrane segments of voltage-gated potassium chann...
AbstractThe activation of Shaker K+ channels is steeply voltage dependent. To determine whether cons...
AbstractVoltage-activated ion channels respond to changes in membrane voltage by coupling the moveme...
Activation of voltage-dependent channels involves charge-moving conformational changes of the voltag...
In voltage-dependent channels, positive charges contained within the S4 domain are the voltage-sensi...
AbstractThe S4 segment comprises part of the voltage sensor in Shaker K+ channels. We have used a st...
In voltage-dependent Shaker K+ channels, charged residues E293 in transmembrane segment S2 and R365,...
AbstractVoltage-activated ion channels respond to changes in membrane voltage by coupling the moveme...
Activation of voltage-dependent channels involves charge-moving conformational changes of the voltag...
Using a strategy related to intragenic suppression, we previously obtained evidence for structural i...
The structural organization of the voltage sensor in K+ channels has been investigated by second sit...
Using a strategy related to intragenic suppression, we previously obtained evidence for structural i...
The highly conserved fourth transmembrane segment (S4) is the primary voltage sensor of the voltage-...
AbstractIn voltage-dependent ion channels, pore opening is initiated by electrically driven movement...
The S4 transmembraneα-helix in voltage-gated channels contains several regularly spaced basic amino ...
ABSTRACT The cytoplasmic ends of the four S6 transmembrane segments of voltage-gated potassium chann...
AbstractThe activation of Shaker K+ channels is steeply voltage dependent. To determine whether cons...
AbstractVoltage-activated ion channels respond to changes in membrane voltage by coupling the moveme...
Activation of voltage-dependent channels involves charge-moving conformational changes of the voltag...
In voltage-dependent channels, positive charges contained within the S4 domain are the voltage-sensi...
AbstractThe S4 segment comprises part of the voltage sensor in Shaker K+ channels. We have used a st...
In voltage-dependent Shaker K+ channels, charged residues E293 in transmembrane segment S2 and R365,...
AbstractVoltage-activated ion channels respond to changes in membrane voltage by coupling the moveme...
Activation of voltage-dependent channels involves charge-moving conformational changes of the voltag...
Using a strategy related to intragenic suppression, we previously obtained evidence for structural i...
The structural organization of the voltage sensor in K+ channels has been investigated by second sit...
Using a strategy related to intragenic suppression, we previously obtained evidence for structural i...
The highly conserved fourth transmembrane segment (S4) is the primary voltage sensor of the voltage-...
AbstractIn voltage-dependent ion channels, pore opening is initiated by electrically driven movement...
The S4 transmembraneα-helix in voltage-gated channels contains several regularly spaced basic amino ...
ABSTRACT The cytoplasmic ends of the four S6 transmembrane segments of voltage-gated potassium chann...