AbstractThe single-channel conductance varies significantly between different members of the inward rectifier (Kir) family of potassium channels. Mutations at three sites in Kir6.2 have been shown to produce channels with reduced single-channel conductance, the largest reduction (to 40% of wild-type) being for V127T. We have used homology modeling (based on a KcsA template) combined with molecular dynamics simulations in a phosphatidycholine bilayer to explore whether changes in structural dynamics of the filter were induced by three such mutations: V127T, M137C, and G135F. Overall, 12 simulations of Kir6.2 models, corresponding to a total simulation time of 27ns, have been performed. In these simulations we focused on distortions of the se...
AbstractUsing the experimentally determined KcsA structure as a template, we propose a plausible exp...
Potassium channels have been studied intensively in terms of the relationship between molecular stru...
AbstractPotassium channels display a high conservation of sequence of the selectivity filter (SF), y...
AbstractThe single-channel conductance varies significantly between different members of the inward ...
AbstractThe bacterial channel KirBac1.1 provides a structural homolog of mammalian inward rectifier ...
AbstractA homology model has been generated for the pore-forming domain of Kir6.2, a component of an...
The bacterial channel KirBac1.1 provides a structural homolog of mammalian inward rectifier potassiu...
ABSTRACT A homology model has been generated for the pore-forming domain of Kir6.2, a component of a...
Biological ion channels are protein pores of sub-nanometer radius that enable rapid movement of sele...
AbstractInteractions of Na+, K+, Rb+, and Cs+ ions within the selectivity filter of a potassium chan...
Inward rectifier potassium (Kir) channels regulate cell excitability and transport K+ ions across me...
AbstractInward rectifier (Kir) potassium channels are characterized by two transmembrane helices per...
ABSTRACT: Inward rectifier potassium (Kir) channels regulate cell excitability and transport K+ ions...
AbstractPotassium channels have been studied intensively in terms of the relationship between molecu...
Molecular modeling and simulations enable extrapolation for the structure of bacterial potassium cha...
AbstractUsing the experimentally determined KcsA structure as a template, we propose a plausible exp...
Potassium channels have been studied intensively in terms of the relationship between molecular stru...
AbstractPotassium channels display a high conservation of sequence of the selectivity filter (SF), y...
AbstractThe single-channel conductance varies significantly between different members of the inward ...
AbstractThe bacterial channel KirBac1.1 provides a structural homolog of mammalian inward rectifier ...
AbstractA homology model has been generated for the pore-forming domain of Kir6.2, a component of an...
The bacterial channel KirBac1.1 provides a structural homolog of mammalian inward rectifier potassiu...
ABSTRACT A homology model has been generated for the pore-forming domain of Kir6.2, a component of a...
Biological ion channels are protein pores of sub-nanometer radius that enable rapid movement of sele...
AbstractInteractions of Na+, K+, Rb+, and Cs+ ions within the selectivity filter of a potassium chan...
Inward rectifier potassium (Kir) channels regulate cell excitability and transport K+ ions across me...
AbstractInward rectifier (Kir) potassium channels are characterized by two transmembrane helices per...
ABSTRACT: Inward rectifier potassium (Kir) channels regulate cell excitability and transport K+ ions...
AbstractPotassium channels have been studied intensively in terms of the relationship between molecu...
Molecular modeling and simulations enable extrapolation for the structure of bacterial potassium cha...
AbstractUsing the experimentally determined KcsA structure as a template, we propose a plausible exp...
Potassium channels have been studied intensively in terms of the relationship between molecular stru...
AbstractPotassium channels display a high conservation of sequence of the selectivity filter (SF), y...