Hydrogen-deuterium exchange study of amino acids and proteins by 200- to 230-nm spectroscopy

Deuteration of asparagine, glutamine, arginine, tryptophan, and tyrosine has been found to cause a small but appreciable spectral change in the 200- to 230-nm region. By the use of a stopped-flow ultraviolet absorption method, the rates of deuteration of these amino acids have been determined. On the basis of these results, and on the basis of our previous study on the hydrogen-deuterium exchange of the peptide groups, a few comments are given as for how to apply the method to protein study.