Article
High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspartic acids and structural implications of single site mutations.
European biophysics journal : EBJ - 1 Jan 1990
Engelhard M, Hess B, Metz G, Kreutz W, Siebert F, Soppa J, Oesterhelt D
Abstract excerpt
Three mutant strains of Halobacterium sp. GRB with the site of mutation in the bacterioopsin gene (PM 326: Asp96----Asn; PM 374: Asp96----Gly; PM 384: Asp85----Glu) were grown in a synthetic medium containing (4-13C)-Asp. The mutant bacteriorhodopsins labeled with (4-13C)-Asp (37%-45%), and owing to the metabolism of Halobacteria also with (11-13C)-Trp (50%-100%), were isolated as purple membranes and 13C Solid...
Topics
- Aspartic Acid
- Bacteriorhodopsins
- Carbon Isotopes
- Glutamates
- Glutamic Acid
- Glycine
- Halobacterium
- Magnetic Resonance Spectroscopy
- Mutation
- Tryptophan