Article
The hinge portion of the S. aureus alpha-toxin crosses the lipid bilayer and is part of the trans-mouth of the channel.
Biochimica et biophysica acta - 2 Oct 1997
Krasilnikov O V, Yuldasheva L N, Merzlyak P G, Capistrano M F, Nogueira R A
Abstract excerpt
This paper compares the functional properties of ion channels formed in planar lipid membranes by the wild and mutant Staphylococcus aureus alpha-toxin. It was shown that replacement of the amino acid Gly at position 130 by Cys in the primary structure of the toxin decreases the single-channel conductance with a concomitant decrease in the pH at which the channel becomes unable to discriminate between Cl- and K+...
Topics
- Bacterial Toxins
- Electric Conductivity
- Electrophysiology
- Glucose
- Hemolysin Proteins
- Hydrogen-Ion Concentration
- Ion Channels
- Lipid Bilayers
- Membrane Potentials
- Mutation
- Particle Size
- Phosphatidylcholines
- Phospholipids
- Polyethylene Glycols
- Staphylococcus aureus
- Sucrose