Dimerization of TonB is not essential for its binding to the outer membrane siderophore receptor FhuA of Escherichia coli. [electronic resource]
Producer: 20040519Description: 9978-86 p. digitalISSN:- 0021-9258
- Amino Acid Sequence
- Bacterial Outer Membrane Proteins -- chemistry
- Bacterial Proteins -- chemistry
- Bacteriophages -- chemistry
- Cell Division
- Cytoplasm -- metabolism
- Dimerization
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli -- metabolism
- Escherichia coli Proteins -- chemistry
- Ferrichrome -- chemistry
- Hydrogen-Ion Concentration
- Membrane Proteins -- chemistry
- Models, Molecular
- Molecular Sequence Data
- Plasmids -- metabolism
- Protein Binding
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Protons
- Receptors, Virus -- chemistry
- Siderophores -- metabolism
- Spectrometry, Fluorescence
- Tryptophan -- chemistry
- Ultracentrifugation
No physical items for this record
Publication Type: Journal Article
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