title: Selectively deuterated amino acid analogues. Synthesis, incorporation into proteins and NMR properties.
abstract: Selectively deuterated analogues of histidine, tyrosine, phenylalanine and tryptophan have been synthesized by chemical exchange. These analogues have been characterized by NMR spectrometry and used for growth of bacteria. Active lactose repressor protein has been isolated from cells grown on the deuterated amino acids, and denatured 1H and 2H NMR spectra have been determined for the protein.
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D001426:Bacterial Proteins / Q000096:biosynthesis*; D055598:Chemical Phenomena; D002621:Chemistry; D003903:Deuterium; D004794:Enzyme Repression; D004926:Escherichia coli / Q000378:metabolism; D006639:Histidine / Q000031:analogs & derivatives; D007553:Isotope Labeling; D009682:Magnetic Resonance Spectroscopy; D010649:Phenylalanine / Q000031:analogs & derivatives; D014364:Tryptophan / Q000031:analogs & derivatives; D014443:Tyrosine / Q000031:analogs & derivatives
chemical_list: D000596:Amino Acids; D001426:Bacterial Proteins; D014443:Tyrosine; D010649:Phenylalanine; D006639:Histidine; D014364:Tryptophan; D003903:Deuterium