A method has been developed to obtain well-defined NMR spectra of a structural lipoprotein of Escherichia coli in situ. When a histidine- and tryptophan-requiring strain was starved of both histidine and tryptophan, the lipoprotein was the only protein produced in the membrane. Using this condition, the lipoprotein, which has only one tyrosine residue (at the 56th position), was labeled with m-fluorotyrosine or 2-13C-tyrosine. The NMR spectra of the membrane fractions thus obtained have rather sharp peaks, indicating that the labeled side chains are relatively mobile, in agreement with the results of our ESR studies on the carboxyl-terminal region of the lipoprotein.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Oct 24 1977|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology