Affiliation: | (1) Dept. of Genetics and Genomics, Boston University School of Medicine, Boston University, 715 Albany St., E639, Boston, MA 02118, USA;(2) Dept. of Genetics, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115, USA;(3) The Lipper Center for Computational Genetics. Harvard Medical School, 200 Longwood Ave., Boston, MA 02115, USA;(4) Dept. of Biomedical Engineering, Boston University, 44 Cummington St., Boston, MA 02215, USA |
Abstract: | Background The observed molecular weight of a protein on a 1D polyacrylamide gel can provide meaningful insight into its biological function. Differences between a protein's observed molecular weight and that predicted by its full length amino acid sequence can be the result of different types of post-translational events, such as alternative splicing (AS), endoproteolytic processing (EPP), and post-translational modifications (PTMs). The characterization of these events is one of the important goals of total proteome profiling (TPP). LC/MS/MS has emerged as one of the primary tools for TPP, but since this method identifies tryptic fragments of proteins, it has not generally been used for large-scale determination of the molecular weight of intact proteins in complex mixtures. |