Analysis of Post Translational Modification of Proteins, Phosphorylation, Glycosylation, Sulphation, Genomic Sequence

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Analysis of post-translational modification of proteins

Post-translational modification of proteins involves phosphorylation, glycosylation, sulphation, etc., which are extremely important for protein function. These modifications can not be inferred from genomic sequences or cDNA sequences. For this purpose, all peptides having unexpected molecular mass need to be analysed further. This is not easy, although continuous progress is being made in this area. For instance, phosphorylation events can be studied using the following criteria:

(i) It is known that phosphopeptides (phosphorylated at one amino acid residue) are 80Da heavier than their unmodified counterparts. (ii) A phosphopeptide with a single phosphate group will release a phosphate group (POs, mass 79) due to phosphatase treatment. (iii) Phosphopeptide bind to metal resins and are recognized by specific antibodies.

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