The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition. [electronic resource]
Producer: 20120322Description: 781-91 p. digitalISSN:- 0973-7138
- Amino Acid Sequence
- Cnidarian Venoms -- chemical synthesis
- Hydrophobic and Hydrophilic Interactions
- Lipid Bilayers -- chemistry
- Membrane Lipids -- chemistry
- Molecular Sequence Data
- Organic Chemicals -- chemical synthesis
- Peptide Fragments -- chemical synthesis
- Permeability
- Protein Binding
- Unilamellar Liposomes -- chemistry
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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