title: Electron transfer dissociation mass spectrometry in proteomics.
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.
authors.affiliation: Department of Biological Chemistry, McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
authors.forename: Min-Sik
authors.initials: MS
authors.lastname: Kim
authors.forename: Akhilesh
authors.initials: A
authors.lastname: Pandey
mesh_terms: D013058:Mass Spectrometry / Q000379:methods; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D046188:Protein Modification, Translational; D011506:Proteins / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D020539:Sequence Analysis, Protein / Q000379:methods*
chemical_list: D010455:Peptides; D011506:Proteins