Add to ORKGhar rop ne. fs s omm in actions with acidic side chains at a central site capped by Kv and related channels, namely KvAP from Aeropyrum (20). Phospholipids such as DOPC (1,2-dioleoyl-glycero-activated VS domains of Kv2.1 (27), appearing to (which removes the entire headgroup of the sphingolipid) immobilizes the VS in the resting state (28). Interestingly
A number of membrane proteins act via binding at the water/lipid bilayer interface. An important exa...
Most membrane proteins contain a transmembrane (TM) domain made up of a bundle of lipid-bilayer-span...
Molecular dynamics (MO) simulations were used to study the interaction of voltage-gated potassium (K...
AbstractVoltage sensors (VS) domains couple the activation of ion channels/enzymes to changes in mem...
Voltage sensors (VS) domains couple the activation of ion channels/enzymes to changes in membrane vo...
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 ...
SummaryA strong interplay between the voltage-sensor domain (VSD) and the pore domain (PD) underlies...
Coarse-grained molecular dynamics simulations are used to explore the interaction with a phospholipi...
AbstractThe membrane location of two fragments in two different K+-channels, the KvAP (from Aeropyru...
AbstractCells commonly use lipids to modulate the function of ion channels. The lipid content influe...
VSTx1 is a tarantula venom toxin which binds to the archaebacterial voltage-gated potassium channel ...
AbstractVoltage-sensor (VS) domains cause the pore of voltage-gated ion channels to open and close i...
AbstractThe S4 transmembrane segment in voltage-gated ion channels, a highly basic α helix, responds...
Pant et al. describe the mechanism by which PIP2 might regulate homomeric Kv7.2 channels. They ident...
A number of membrane proteins act via binding at the water/lipid bilayer interface. An important exa...
Most membrane proteins contain a transmembrane (TM) domain made up of a bundle of lipid-bilayer-span...
Molecular dynamics (MO) simulations were used to study the interaction of voltage-gated potassium (K...
AbstractVoltage sensors (VS) domains couple the activation of ion channels/enzymes to changes in mem...
Voltage sensors (VS) domains couple the activation of ion channels/enzymes to changes in membrane vo...
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 ...
SummaryA strong interplay between the voltage-sensor domain (VSD) and the pore domain (PD) underlies...
Coarse-grained molecular dynamics simulations are used to explore the interaction with a phospholipi...
AbstractThe membrane location of two fragments in two different K+-channels, the KvAP (from Aeropyru...
AbstractCells commonly use lipids to modulate the function of ion channels. The lipid content influe...
VSTx1 is a tarantula venom toxin which binds to the archaebacterial voltage-gated potassium channel ...
AbstractVoltage-sensor (VS) domains cause the pore of voltage-gated ion channels to open and close i...
AbstractThe S4 transmembrane segment in voltage-gated ion channels, a highly basic α helix, responds...
Pant et al. describe the mechanism by which PIP2 might regulate homomeric Kv7.2 channels. They ident...
A number of membrane proteins act via binding at the water/lipid bilayer interface. An important exa...
Most membrane proteins contain a transmembrane (TM) domain made up of a bundle of lipid-bilayer-span...
Molecular dynamics (MO) simulations were used to study the interaction of voltage-gated potassium (K...