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...
Autors principals: | Domene, C, Vemparala, S, Klein, M, Vénien-Bryan, C, Doyle, D |
---|---|
Format: | Journal article |
Idioma: | English |
Publicat: |
2006
|
Ítems similars
-
Role of aromatic localization in the gating process of a potassium channel.
per: Domene, C, et al.
Publicat: (2006) -
Interaction of anesthetics with open and closed conformations of a potassium channel studied via molecular dynamics and normal mode analysis.
per: Vemparala, S, et al.
Publicat: (2008) -
Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography.
per: Kuo, A, et al.
Publicat: (2005) -
Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography.
per: Kuo, A, et al.
Publicat: (2005) -
Conformational changes and gating at the selectivity filter of potassium channels.
per: Domene, C, et al.
Publicat: (2008)