Nature and extent of peptide bond cleavage by anhydrous heptafluorobutyric acid during Edman degradation.
It is well established that during the isothiocyanate degradation of proteins a gradual increase of the level of all thiohydantoin derivatives of amino acids occurs, which progressively obscures the sequential identification of the significant N-terminal amino acids. The major cause for this has been shown to be due to a hitherto unknown specific cleavage at aspartic acid residues in anhydrous heptafluorobutyric acid and to a lesser extent, the N leads to O shift in peptide bonds involving hydroxyamino acids. Measures to reduce the susceptibility of the peptide bonds at these sites are described.
D000595:Amino Acid Sequence; D002087:Butyrates / Q000494:pharmacology*; D010443:Peptide Chain Termination, Translational
D002087:Butyrates