Article
Tetramethylrhodamine dimer formation as a spectroscopic probe of the conformation of Escherichia coli ribosomal protein L7/L12 dimers.
The Journal of biological chemistry - 29 Mar 1996
Hamman B D, Oleinikov A V, Jokhadze G G, Bochkariov D E, Traut R R, Jameson D M
Abstract excerpt
The fluorescent probe tetramethylrhodamine iodoacetamide was attached to cysteine residues substituted at various specific locations in full-length and deletion variants of the homodimeric Escherichia coli ribosomal protein L7/L12. Ground-state tetramethylrhodamine dimers form between the two subunits of L7/L12 depending upon the location of the probe. The formation of tetramethylrhodamine dimers caused the...
Topics
- Binding Sites
- Cysteine
- Escherichia coli
- Fluorescent Dyes
- Genetic Variation
- Macromolecular Substances
- Models, Structural
- Protein Conformation
- Rhodamines
- Ribosomal Protein L10
- Ribosomal Proteins
- Ribosomes
- Sequence Deletion