Cargando…
Protein Translocation across Planar Bilayers by the Colicin Ia Channel-Forming Domain: Where Will It End?
Colicin Ia, a 626-residue bactericidal protein, consists of three domains, with the carboxy-terminal domain (C domain) responsible for channel formation. Whole colicin Ia or C domain added to a planar lipid bilayer membrane forms voltage-gated channels. We have shown previously that the channel form...
Autores principales: | Kienker, Paul K., Jakes, Karen S., Finkelstein, Alan |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2000
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2230624/ https://www.ncbi.nlm.nih.gov/pubmed/11004207 |
Ejemplares similares
-
Sizing the Protein Translocation Pathway of Colicin Ia Channels
por: Kienker, Paul K., et al.
Publicado: (2003) -
Identification of Channel-lining Amino Acid Residues in the Hydrophobic Segment of Colicin Ia
por: Kienker, Paul K., et al.
Publicado: (2008) -
The Diphtheria Toxin Channel-forming T Domain Translocates Its Own NH(2)-Terminal Region Across Planar Bilayers
por: Senzel, Lisa, et al.
Publicado: (1998) -
Identification of a translocated gating charge in a voltage-dependent channel. Colicin E1 channels in planar phospholipid bilayer membranes
Publicado: (1991) -
Major transmembrane movement associated with colicin Ia channel gating
Publicado: (1996)