Article
Dimerization of a His117Gly azurin mutant by external addition of 1,omega-di(imidazol-1-yl)alkanes.
Biochemistry - 8 Oct 1996
van Pouderoyen G, den Blaauwen T, Reedijk J, Canters G W
Abstract excerpt
The possibility to construct non-covalently linked protein dimers was investigated by employing the His117Gly mutant of the Cu containing azurin and the bifunctional 1,omega-di(imidazol-1-yl)alkanes as linkers. The His117Gly mutation creates a gap in the coordination sphere of the metal through w...
Topics
- Alkanes
- Azurin
- Copper
- Cross-Linking Reagents
- Dimerization
- Electron Spin Resonance Spectroscopy
- Imidazoles
- Ligands
- Models, Molecular
- Mutation
- Protein Binding
- Protein Conformation
- Protein Structure, Secondary
- Pseudomonas aeruginosa
- Recombinant Proteins
- Spectrophotometry
- Thermodynamics