19F-and 13C-NMR studies of a specifically labelled lipoprotein in the Eschericia coli membrane

Nancy Lee, Masayori Inouye, Paul C. Lauterbur

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

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 languageEnglish (US)
Pages (from-to)1211-1218
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume78
Issue number4
DOIs
StatePublished - Oct 24 1977
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of '<sup>19</sup>F-and <sup>13</sup>C-NMR studies of a specifically labelled lipoprotein in the Eschericia coli membrane'. Together they form a unique fingerprint.

Cite this