[1] One application of the technique includes detection of protein modifications in two bacterial species Ehrlichia- E. muris and IOE.
The technique showed that the antigenic proteins of the non-virulent E.muris is more post-translationally modified than the highly virulent IOE.
The nascent or folded proteins, which are stable under physiological conditions, are then subjected to a battery of specific enzyme-catalyzed modifications on the side chains or backbones.
Post-translational modification of proteins can include acetylation, acylation (myristoylation, palmitoylation), alkylation, arginylation, ADP-ribosylation, biotinylation, formylation, geranylgeranylation, glutamylation, glycosylation, glycylation, hydroxylation, isoprenylation, lactylation, lipoylation, methylation, nitroalkylation, phosphopantetheinylation, phosphorylation, prenylation, selenation, S-nitrosylation, succinylation, sulfation, transglutamination, sulfinylation, sulfonylation and ubiquitination (sumoylation, neddylation).
[28][29] Post-translational modifications occurring at the N-terminus of the amino acid chain play an important role in translocation across biological membranes.