Abstract
The nominal mass of amino acid residues calculated from their elemental compositions are defined by prime numbers far more often than chance, and such residues appear to play an important role in the formation and biology of proteins. It is proposed therefore that consideration be given to classifying prime mass amino acids as such, beyond the more common, familiar definitions associated with the other physicochemical properties of amino acids including charged or non-charged, hydrophobic or hydrophilic, polar or non-polar, acidic or basic, aliphatic or aromatic. Greater focus could also be given to such residues during peptide and protein sequencing with mass spectrometry and the construction of structural maps, given their predominantly hydrophobic character and thus their role in protein folding and transmembrane domains. The use of prime numbers to define amino acids based on the sum of the atomic masses from their elemental compositions invokes other recent interest and observations whereby prime numbers were organised in a way that mirrors electrons arranged within the orbitals of an atom. The article links number theory with both the physical and biological sciences, and mass spectrometry, for the first time.