AbstractThe structure of the bacterial potassium channel, KcsA, corresponds to the channel in a closed state. Two lines of evidence suggest that the channel must widen its intracellular mouth when in an open state: 1) internal block by a series of tetraalkylammonium ions and 2) spin labeling experiments. Thus it is known that the protein moves in this region, but it is unclear by how much and the mechanisms that are involved. To address this issue we have applied a novel approach to generate plausible open-state models of KcsA. The approach can be thought of as placing a balloon inside the channel and gradually inflating it. Only the protein sees the balloon, and so water is free to move in and out of the channel. The balloon is a van der W...
The bacterial K+ channel KcsA can be used to help elucidate questions about channel inactivation and...
AbstractThe structural, dynamical, and thermodynamic properties of a model potassium channel are stu...
ABSTRACT Potassium channels enable K1 ions to move passively across biological membranes. Multiple n...
The structure of the bacterial potassium channel, KcsA, corresponds to the channel in a closed state...
AbstractThe structure of the bacterial potassium channel, KcsA, corresponds to the channel in a clos...
Bacterial homologues of mammalian potassium channels provide structures of two states of a gated K c...
The gating mechanism of a bacterial potassium channel, KcsA, has been investigated via multi-nanosec...
<div><p>The bacterial potassium channel KcsA, which has been crystallized in several conformations, ...
AbstractUsing the experimentally determined KcsA structure as a template, we propose a plausible exp...
The mechanisms underlying transport of ions across the potassium channel are examined using electros...
Potassium channels enable K(+) ions to move passively across biological membranes. Multiple nanoseco...
The mechanisms underlying transport of ions across the potassium channel are examined using electros...
Potassium channels have been studied intensively in terms of the relationship between molecular stru...
AbstractThe mechanisms underlying transport of ions across the potassium channel are examined using ...
The structural, dynamical, and thermodynamic properties of a model potassium channel are studied usi...
The bacterial K+ channel KcsA can be used to help elucidate questions about channel inactivation and...
AbstractThe structural, dynamical, and thermodynamic properties of a model potassium channel are stu...
ABSTRACT Potassium channels enable K1 ions to move passively across biological membranes. Multiple n...
The structure of the bacterial potassium channel, KcsA, corresponds to the channel in a closed state...
AbstractThe structure of the bacterial potassium channel, KcsA, corresponds to the channel in a clos...
Bacterial homologues of mammalian potassium channels provide structures of two states of a gated K c...
The gating mechanism of a bacterial potassium channel, KcsA, has been investigated via multi-nanosec...
<div><p>The bacterial potassium channel KcsA, which has been crystallized in several conformations, ...
AbstractUsing the experimentally determined KcsA structure as a template, we propose a plausible exp...
The mechanisms underlying transport of ions across the potassium channel are examined using electros...
Potassium channels enable K(+) ions to move passively across biological membranes. Multiple nanoseco...
The mechanisms underlying transport of ions across the potassium channel are examined using electros...
Potassium channels have been studied intensively in terms of the relationship between molecular stru...
AbstractThe mechanisms underlying transport of ions across the potassium channel are examined using ...
The structural, dynamical, and thermodynamic properties of a model potassium channel are studied usi...
The bacterial K+ channel KcsA can be used to help elucidate questions about channel inactivation and...
AbstractThe structural, dynamical, and thermodynamic properties of a model potassium channel are stu...
ABSTRACT Potassium channels enable K1 ions to move passively across biological membranes. Multiple n...