Article
Wild-type and mutant bacteriorhodopsins D85N, D96N, and R82Q: purification to homogeneity, pH dependence of pumping, and electron diffraction.
Biochemistry - 26 Mar 1991
Miercke L J, Betlach M C, Mitra A K, Shand R F, Fong S K, Stroud R M
Abstract excerpt
Bacterioopsin, expressed in Escherichia coli as a fusion protein with 13 heterologous residues at the amino terminus, has been purified in the presence of detergents and retinylated to give bacteriorhodopsin. Further purification yielded pure bacteriorhodopsin, which had an absorbance ratio (A280/A lambda max) of 1.5 in the dark-adapted state in a single-detergent environment. This protein has a folding rate,...
Topics
- Bacteriorhodopsins
- Crystallization
- Electrons
- Electrophoresis, Polyacrylamide Gel
- Escherichia coli
- Gene Expression Regulation, Bacterial
- Genes, Bacterial
- Hydrogen-Ion Concentration
- Microscopy, Electron
- Mutation