Site-specific 15N-labelling of oligonucleotides for NMR: the trp operator and its interaction with the trp repressor.
A convenient and economical method is described for the site-specific 15N-labelling of the 4-amino group of individual cytidine residues in oligonucleotides. This is applied to a 20 base-pair oligonucleotide corresponding to the trp operator; this oligonucleotide and its complex with the E. coli trp repressor are studied by NMR, using 1H-15N HMQC and 15N-edited 1H-1H NOESY experiments.
Ramesh
V
V
Department of Biochemistry and Biological NMR Centre, University of Leicester, UK.
Xu
Y Z
YZ
Roberts
G C
GC
D001426:Bacterial Proteins; D001483:Base Sequence; D006860:Hydrogen Bonding; D007553:Isotope Labeling; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009587:Nitrogen Isotopes; D009690:Nucleic Acid Conformation; D009841:Oligonucleotides / Q000737:chemistry* / Q000378:metabolism; D009876:Operon; D012097:Repressor Proteins / Q000737:chemistry* / Q000378:metabolism; D014364:Tryptophan / Q000235:genetics*; D029968:Escherichia coli Proteins
D001426:Bacterial Proteins; D009587:Nitrogen Isotopes; D009841:Oligonucleotides; D012097:Repressor Proteins; D014364:Tryptophan; C027190:TRPR protein, E coli; D029968:Escherichia coli Proteins