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Electron transfer dissociation mass spectrometry in proteomics

Authors

  • Min-Sik Kim,

    1. Johns Hopkins University School of Medicine, McKusick-Nathans Institute of Genetic Medicine and Department of Biological Chemistry, Baltimore, MD, USA
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  • Akhilesh Pandey

    Corresponding author
    1. Johns Hopkins University School of Medicine, McKusick-Nathans Institute of Genetic Medicine and Department of Biological Chemistry, Baltimore, MD, USA
    2. Johns Hopkins University School of Medicine, Departments of Pathology and Oncology, Baltimore, MD, USA
    • McKusick-Nathans Institute of Genetic Medicine and Departments of Biological Chemistry, Pathology and Oncology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA, Fax: +1-410-502-7544
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Abstract

Mass spectrometry has rapidly evolved to become the platform of choice for proteomic analysis. While CID remains the major fragmentation method for peptide sequencing, electron transfer dissociation (ETD) is emerging as a complementary method for the characterization of peptides and post-translational modifications (PTMs). Here, we review the evolution of ETD and some of its newer applications including characterization of PTMs, non-tryptic peptides and intact proteins. We will also discuss some of the unique features of ETD such as its complementarity with CID and the use of alternating CID/ETD along with issues pertaining to analysis of ETD data. The potential of ETD for applications such as multiple reaction monitoring and proteogenomics in the future will also be discussed.

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