%0 Journal Article %1 matthews_selectively_1977 %A Matthews, H R %A Matthews, K S %A Opella, S J %D 1977 %J Biochim. Biophys. Acta %K Acids,Bacterial Amino Labeling,Magnetic Phenomena,Chemistry,Deuterium,Enzyme Proteins,Chemical Repression,Escherichia Resonance Spectroscopy,Phenylalanine,Tryptophan,Tyrosine coli,Histidine,Isotope %N 1 %P 1--13 %T Selectively deuterated amino acid analogues. \Synthesis\, incorporation into proteins and \NMR\ properties %V 497 %X 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.

@article{matthews_selectively_1977, 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.}, added-at = {2017-03-14T02:48:56.000+0100}, author = {Matthews, H R and Matthews, K S and Opella, S J}, biburl = {https://www.bibsonomy.org/bibtex/2e42150d8f0809fbb80a83c388864edc3/nmrresource}, interhash = {540a6a01d848366dd5831a23c55e046e}, intrahash = {e42150d8f0809fbb80a83c388864edc3}, issn = {0006-3002}, journal = {Biochim. Biophys. Acta}, keywords = {Acids,Bacterial Amino Labeling,Magnetic Phenomena,Chemistry,Deuterium,Enzyme Proteins,Chemical Repression,Escherichia Resonance Spectroscopy,Phenylalanine,Tryptophan,Tyrosine coli,Histidine,Isotope}, month = mar, number = 1, pages = {1--13}, pmid = {321035}, timestamp = {2017-03-14T02:49:21.000+0100}, title = {{Selectively deuterated amino acid analogues. {\{}Synthesis{\}}, incorporation into proteins and {\{}NMR{\}} properties}}, volume = 497, year = 1977 }