Article
Dual Lifetimes for Complexes between Glutathione-S-transferase (hGSTA1-1) and Product-like Ligands Detected by Single-Molecule Fluorescence Imaging.
Biochemistry - 8 Aug 2017
Pettersson John R, Lanni Frederick, Rule Gordon S
Abstract excerpt
Single-molecule fluorescence techniques were used to characterize the binding of products and inhibitors to human glutathione S-transferase A1-1 (hGSTA1-1). The identification of at least two different bound states for the wild-type enzyme suggests that there are at least two conformations of the...
Topics
- Amino Acid Substitution
- Binding Sites
- Biotinylation
- Catalytic Domain
- Enzyme Inhibitors
- Enzyme Stability
- Fluorescence Polarization
- Fluorescence Resonance Energy Transfer
- Fluorescent Dyes
- Glutathione
- Glutathione Transferase
- Humans
- Image Processing, Computer-Assisted
- Kinetics
- Ligands
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation