Article
The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.
PloS one - 1 Jan 2014
Benz Roland, Maier Elke, Bauer Susanne, Ludwig Albrecht
Abstract excerpt
Escherichia coli α-hemolysin (HlyA) is a pore-forming protein of 110 kDa belonging to the family of RTX toxins. A hydrophobic region between the amino acid residues 238 and 410 in the N-terminal half of HlyA has previously been suggested to form hydrophobic and/or amphipathic α-helices and has been shown to be important for hemolytic activity and pore formation in biological and artificial membranes. The...
Topics
- DNA Primers
- Erythrocytes
- Escherichia coli
- Escherichia coli Proteins
- Gene Deletion
- Hemolysin Proteins
- Hemolysis
- Lipid Bilayers
- Lipids
- Membranes, Artificial
- Mutagenesis, Site-Directed
- Mutation
- Osmosis
- Plasmids
- Porins