Selective isotope labeling of recombinant proteins in escherichia coli

Kit I. Tong, Masayuki Yamamoto, Toshiyuki Tanaka

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Citations (Scopus)

Abstract

Selective stable-isotope labeling is a useful technique to study structures of proteins, especially intrinsically disordered proteins, by nuclear magnetic resonance spectroscopy. Here, we describe a simple method for amino acid selective isotope labeling of recombinant proteins in E. coli. This method only requires addition of an excess of unlabeled amino acids and, if necessary, enzyme inhibitors to the culture medium. Its efficiency has been demonstrated even in labeling with glutamine or glutamate that is easily converted to other amino acid types by the metabolic pathways of E. coli.

Original languageEnglish
Title of host publicationIntrinsically Disordered Protein Analysis
Subtitle of host publicationVolume 2, Methods and Experimental Tools
EditorsVladimir Uversky, Vladimir Uversky, Keith Dunker
Pages439-448
Number of pages10
DOIs
Publication statusPublished - 2012

Publication series

NameMethods in Molecular Biology
Volume896
ISSN (Print)1064-3745

Keywords

  • Amino acid selective isotope labeling
  • Intrinsically disordered protein
  • N-Glutamate labeling
  • N-Glutamine labeling

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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