Article
Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. 2. Site-directed fluorescence studies.
Biochemistry - 11 Oct 1994
Wu J, Kaback H R
Abstract excerpt
By using site-directed fluorescence spectroscopy, we have carried out structure/function studies on lactose permease purified from Escherichia coli in dodecyl beta, D-maltoside. Initially, permease containing a single native Cys at position 148 (helix V) was studied, since this residue is protect...
Topics
- Anilino Naphthalenesulfonates
- Base Sequence
- Binding Sites
- Cysteine
- Escherichia coli
- Escherichia coli Proteins
- Galactose
- Lactose
- Ligands
- Membrane Transport Proteins
- Molecular Sequence Data
- Monosaccharide Transport Proteins
- Mutagenesis, Site-Directed
- Mutation
- Protein Structure, Secondary
- Spectrometry, Fluorescence
- Structure-Activity Relationship
- Sulfhydryl Reagents