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. 1977 Mar 29;497(1):1-13.
doi: 10.1016/0304-4165(77)90134-9.

Selectively deuterated amino acid analogues. Synthesis, incorporation into proteins and NMR properties

H R Matthews, K S Matthews, S J Opella

Selectively deuterated amino acid analogues. Synthesis, incorporation into proteins and NMR properties

H R Matthews et al. Biochim Biophys Acta. .

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.

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