Molecular weight assessment of proteins in total proteome profiles using 1D-PAGE and LC/MS/MS |
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| Authors: | Q?Rushdy?Ahmad Dat?H?Nguyen Mark?A?Wingerd George?M?Church Email author" target="_blank">Martin?A?SteffenEmail author |
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| Institution: | (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 |
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| 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. |
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