SummaryThe nature of voltage sensing by voltage-activated ion channels is a key problem in membrane protein structural biology. The way in which the voltage-sensor (VS) domain interacts with its membrane environment remains unclear. In particular, the known structures of Kv channels do not readily explain how a positively charged S4 helix is able to stably span a lipid bilayer. Extended (2 × 50 ns) molecular dynamics simulations of the high-resolution structure of the isolated VS domain from the archaebacterial potassium channel KvAP, embedded in zwitterionic and in anionic lipid bilayers, have been used to explore VS/lipid interactions at atomic resolution. The simulations reveal penetration of water into the center of the VS and bilayer. ...
SummaryVoltage-activated potassium (Kv) channels contain a central pore domain that is partially sur...
AbstractVoltage sensor domains (VSD) are transmembrane proteins that respond to changes in membrane ...
Ion channels are present in every domain of life. They catalyze the rapid and selective flux of ions...
The nature of voltage sensing by voltage-activated ion channels is a key problem in membrane protein...
SummaryThe nature of voltage sensing by voltage-activated ion channels is a key problem in membrane ...
AbstractVoltage sensors (VS) domains couple the activation of ion channels/enzymes to changes in mem...
Coarse-grained molecular dynamics simulations are used to explore the interaction with a phospholipi...
SummaryA strong interplay between the voltage-sensor domain (VSD) and the pore domain (PD) underlies...
AbstractVoltage-sensor (VS) domains cause the pore of voltage-gated ion channels to open and close i...
Voltage sensors (VS) domains couple the activation of ion channels/enzymes to changes in membrane vo...
AbstractThe recent crystal structures of the voltage-gated potassium channel KvAP and its isolated v...
AbstractIn this article, we present the results of the molecular dynamics simulations of amphiphilic...
AbstractAll-atom molecular dynamics simulations are used to better understand the dynamic environmen...
AbstractA high-resolution crystal structure of KvAP, an archeabacterial voltage-gated potassium (Kv)...
ABSTRACT All-atom molecular dynamics simulations are used to better understand the dynamic environme...
SummaryVoltage-activated potassium (Kv) channels contain a central pore domain that is partially sur...
AbstractVoltage sensor domains (VSD) are transmembrane proteins that respond to changes in membrane ...
Ion channels are present in every domain of life. They catalyze the rapid and selective flux of ions...
The nature of voltage sensing by voltage-activated ion channels is a key problem in membrane protein...
SummaryThe nature of voltage sensing by voltage-activated ion channels is a key problem in membrane ...
AbstractVoltage sensors (VS) domains couple the activation of ion channels/enzymes to changes in mem...
Coarse-grained molecular dynamics simulations are used to explore the interaction with a phospholipi...
SummaryA strong interplay between the voltage-sensor domain (VSD) and the pore domain (PD) underlies...
AbstractVoltage-sensor (VS) domains cause the pore of voltage-gated ion channels to open and close i...
Voltage sensors (VS) domains couple the activation of ion channels/enzymes to changes in membrane vo...
AbstractThe recent crystal structures of the voltage-gated potassium channel KvAP and its isolated v...
AbstractIn this article, we present the results of the molecular dynamics simulations of amphiphilic...
AbstractAll-atom molecular dynamics simulations are used to better understand the dynamic environmen...
AbstractA high-resolution crystal structure of KvAP, an archeabacterial voltage-gated potassium (Kv)...
ABSTRACT All-atom molecular dynamics simulations are used to better understand the dynamic environme...
SummaryVoltage-activated potassium (Kv) channels contain a central pore domain that is partially sur...
AbstractVoltage sensor domains (VSD) are transmembrane proteins that respond to changes in membrane ...
Ion channels are present in every domain of life. They catalyze the rapid and selective flux of ions...