Article
Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function.
Biochemistry - 22 Oct 1991
Hoyt D W, Gierasch L M
Abstract excerpt
Peptides corresponding to the wild-type signal sequence of the Escherichia coli outer membrane protein OmpA and several mutants have been synthesized and characterized biophysically. The mutations were designed collaboratively with Inouye and co-workers to test the understanding of the critical c...
Topics
- Amino Acid Sequence
- Bacterial Outer Membrane Proteins
- Fluoresceins
- Fluorescence Polarization
- Lipids
- Micelles
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Protein Sorting Signals
- Solubility