Electron transfer dissociation mass spectrometry in proteomics

Min Sik Kim, Akhilesh Pandey

Research output: Contribution to journalReview article

77 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)530-542
Number of pages13
JournalProteomics
Volume12
Issue number4-5
DOIs
StatePublished - Feb 1 2012
Externally publishedYes

Fingerprint

Proteomics
Mass spectrometry
Mass Spectrometry
Electrons
Post Translational Protein Processing
Peptides
Monitoring
Proteins

Keywords

  • ETD
  • MRM
  • Non-tryptic peptide
  • O-GlcNAc
  • Proteogenomics
  • Technology

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Electron transfer dissociation mass spectrometry in proteomics. / Kim, Min Sik; Pandey, Akhilesh.

In: Proteomics, Vol. 12, No. 4-5, 01.02.2012, p. 530-542.

Research output: Contribution to journalReview article

Kim, Min Sik ; Pandey, Akhilesh. / Electron transfer dissociation mass spectrometry in proteomics. In: Proteomics. 2012 ; Vol. 12, No. 4-5. pp. 530-542.
@article{4f4654f48517432d80bddf1187d5d835,
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.",
keywords = "ETD, MRM, Non-tryptic peptide, O-GlcNAc, Proteogenomics, Technology",
author = "Kim, {Min Sik} and Akhilesh Pandey",
year = "2012",
month = "2",
day = "1",
doi = "10.1002/pmic.201100517",
language = "English (US)",
volume = "12",
pages = "530--542",
journal = "Proteomics",
issn = "1615-9853",
publisher = "Wiley-VCH Verlag",
number = "4-5",

}

TY - JOUR

T1 - Electron transfer dissociation mass spectrometry in proteomics

AU - Kim, Min Sik

AU - Pandey, Akhilesh

PY - 2012/2/1

Y1 - 2012/2/1

N2 - 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.

AB - 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.

KW - ETD

KW - MRM

KW - Non-tryptic peptide

KW - O-GlcNAc

KW - Proteogenomics

KW - Technology

UR - http://www.scopus.com/inward/record.url?scp=84859222468&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84859222468&partnerID=8YFLogxK

U2 - 10.1002/pmic.201100517

DO - 10.1002/pmic.201100517

M3 - Review article

C2 - 22246976

AN - SCOPUS:84859222468

VL - 12

SP - 530

EP - 542

JO - Proteomics

JF - Proteomics

SN - 1615-9853

IS - 4-5

ER -