By Hermann Dugas
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Additional resources for Bioorganic Chemistry: A Chemical Approach to Enzyme Action
Thus, the reaction of a protein with phenylisothiocyanate provides an important method for the determination of the N-terminal amino acid and subsequent determination of the amino acid sequence ofthe protein. Remembering that the monomeric units of the protein are connected by amide (so-called peptide) linkages, this may be illustrated for the simple dipeptide glycylalanine. As alanine is the leaving group, glycine must be the N-terminal amino acid. The thiohydantoin and alanine formed are easily separated by chromatography, the former being detected by UV absorption and fluorescence.
Further, if the carboxyl function of alanine is also protected, then the only possible reaction is that between the carboxyl (activated) of glycine and the amino of alanine to give the desired dipeptide product. Of course, once the peptide bond is synthesized it becomes necessary to remove the protecting groups under conditions that will not affect the product. Consequently, protecting groups must easily be both attached to the reactants and removed from the product under mild conditions and in high yield.
The fluorine compound is more reactive than the chlorine analogue which might be surprising since the latter is a better leaving group. However, ejection of the leaving group is not the rate-limiting step. Further, the more electronegative fluorine atom will, via inductive pull, offer greater stabilization of 2: Bioorganic Chemistry of the Amino Acids 38 the anionic intermediate, as well as increase the electrophilicity of the carbon atom undergoing nucleophilic attack. Sanger's reagent has unique chromophoric (UV, visible; Amax = 350 nm) properties which further add to its analytical usefulness.