Article
Assignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit. Monitoring conformational changes due to substitutions at position 49.
European journal of biochemistry - 20 May 1990
Sawada S, Akutsu H, Ogasahara K, Yutani K
Abstract excerpt
In order to monitor the conformational changes of tryptophan synthase alpha-subunit from Escherichia coli in solution resulting from amino acid substitutions, we have assigned the Tyr resonances in the aromatic region of the 1H-NMR spectrum to specific residues. In the spectrum of the alpha-subunit deuterated with [2,3,4,5,6-2H5]Phe and [3,5-2H2]Tyr, the C2 and C6 protons of Tyr gave completely isolated signals...
Topics
- Binding Sites
- Escherichia coli
- Glutamine
- Glycine
- Magnetic Resonance Spectroscopy
- Mutation
- Phenylalanine
- Protein Conformation
- Tryptophan Synthase
- Tyrosine