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Enzymatic and mass spectral analysis of mutant and wild‐type selenomethionyl‐dihydrofolate reductase

The site‐specific incorporation of unnatural amino acids, namely selenomethionine, have been incorporated into proteins to facilitate structural studies for over a decade. At times, the stability of selenoproteins is limited due to this biosynthetic incorporation. Wild type and Selenomethionyl dihydrofolate reductase have been prepared and compared for stability and catalytic properties. The sensitivity of wild type and selenomethionyl DHFR to cyanogen bromide and the serine protease trypsin have also been determined to illustrate the application of mass spectral analysis to the study of selenoproteins.