AbstractPotassium channels selectively catalyze potassium transport across cell membranes. Over the past five decades, a multitude of potassium channel models have been proposed. The recent crystal structure determination of the KcsA potassium channel confirms, corrects and expands our understanding of a fundamental biological catalyst, revealing the basis of exquisite selectivity and near diffusion-limited throughput
AbstractPrevious X-ray studies of have focused on the closed state of the potassium channel. Now the...
KcsA, a prokaryote tetrameric potassium channel, was the first ion channel ever to be structurally s...
AbstractA fundamental question associated with the function of ion channels is the conformational ch...
AbstractPotassium channels selectively catalyze potassium transport across cell membranes. Over the ...
AbstractThe determination of the crystal structure of a K+-selective channel protein from Streptomyc...
AbstractCrystal structures have been solved for the transbilayer pore domain of a bacterial K+ chann...
Potassium channels play critical roles in many physiological processes, providing a selective permea...
Potassium channels selectively conduct K+ ions across cellular membranes with extraordinary efficien...
AbstractThe structural, dynamical, and thermodynamic properties of a model potassium channel are stu...
AbstractInteractions of Na+, K+, Rb+, and Cs+ ions within the selectivity filter of a potassium chan...
AbstractUsing the experimentally determined KcsA structure as a template, we propose a plausible exp...
AbstractPotassium channels have been studied intensively in terms of the relationship between molecu...
Our understanding of ion permeation through K+ channels, and by extension through other channels, is...
AbstractThe tetrameric potassium channel from Streptomyces lividans (KcsA) embedded in planar bilaye...
Membrane proteins fascinate at many levels, from their central functional roles in transport, energy...
AbstractPrevious X-ray studies of have focused on the closed state of the potassium channel. Now the...
KcsA, a prokaryote tetrameric potassium channel, was the first ion channel ever to be structurally s...
AbstractA fundamental question associated with the function of ion channels is the conformational ch...
AbstractPotassium channels selectively catalyze potassium transport across cell membranes. Over the ...
AbstractThe determination of the crystal structure of a K+-selective channel protein from Streptomyc...
AbstractCrystal structures have been solved for the transbilayer pore domain of a bacterial K+ chann...
Potassium channels play critical roles in many physiological processes, providing a selective permea...
Potassium channels selectively conduct K+ ions across cellular membranes with extraordinary efficien...
AbstractThe structural, dynamical, and thermodynamic properties of a model potassium channel are stu...
AbstractInteractions of Na+, K+, Rb+, and Cs+ ions within the selectivity filter of a potassium chan...
AbstractUsing the experimentally determined KcsA structure as a template, we propose a plausible exp...
AbstractPotassium channels have been studied intensively in terms of the relationship between molecu...
Our understanding of ion permeation through K+ channels, and by extension through other channels, is...
AbstractThe tetrameric potassium channel from Streptomyces lividans (KcsA) embedded in planar bilaye...
Membrane proteins fascinate at many levels, from their central functional roles in transport, energy...
AbstractPrevious X-ray studies of have focused on the closed state of the potassium channel. Now the...
KcsA, a prokaryote tetrameric potassium channel, was the first ion channel ever to be structurally s...
AbstractA fundamental question associated with the function of ion channels is the conformational ch...