Role of aromatic localization in the gating process of a potassium channel.
Position of the transmembrane aromatic residues of the KirBac1.1 potassium channel shifts from an even distribution in the closed state toward the membrane/solute interface in the open state model. This is the first example of an integral membrane protein making use of the observed preference for tr...
Główni autorzy: | Domene, C, Vemparala, S, Klein, M, Vénien-Bryan, C, Doyle, D |
---|---|
Format: | Journal article |
Język: | English |
Wydane: |
2006
|
Podobne zapisy
-
Role of aromatic localization in the gating process of a potassium channel.
od: Domene, C, i wsp.
Wydane: (2006) -
Interaction of anesthetics with open and closed conformations of a potassium channel studied via molecular dynamics and normal mode analysis.
od: Vemparala, S, i wsp.
Wydane: (2008) -
Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography.
od: Kuo, A, i wsp.
Wydane: (2005) -
Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography.
od: Kuo, A, i wsp.
Wydane: (2005) -
Conformational changes and gating at the selectivity filter of potassium channels.
od: Domene, C, i wsp.
Wydane: (2008)