Cysteine cross-linking defines part of the dimer and B/C domain interface of the Escherichia coli mannitol permease. [electronic resource]
Producer: 20010531Description: 12756-63 p. digitalISSN:- 0021-9258
- Amino Acid Substitution
- Binding Sites
- Copper -- pharmacology
- Cross-Linking Reagents
- Cysteine
- Dimerization
- Disulfides -- analysis
- Escherichia coli -- enzymology
- Escherichia coli Proteins
- Maleimides -- pharmacology
- Mannitol -- metabolism
- Monosaccharide Transport Proteins
- Mutagenesis, Site-Directed
- Oxidation-Reduction
- Phenanthrolines -- pharmacology
- Phosphoenolpyruvate Sugar Phosphotransferase System -- chemistry
- Phosphorylation
- Recombinant Proteins -- chemistry
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
No physical items for this record
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
There are no comments on this title.
Log in to your account to post a comment.