Literature DB >> 15102460

Electron-capture dissociation tandem mass spectrometry.

Roman A Zubarev1.   

Abstract

Electron capture dissociation (ECD) is a new fragmentation technique used in Fourier transform ion cyclotron resonance mass spectrometry and is complementary to traditional tandem mass spectrometry techniques. Disulfide bonds, normally stable to vibrational excitation, are preferentially cleaved in ECD. Fragmentation is fast and specific and labile post-translational modifications and non-covalent bonds often remain intact after backbone bond dissociation. ECD provides more extensive sequence coverage in polypeptides, and at higher electron energies even isoleucine and leucine are distinguishable. In biotechnology, the main area of ECD application is expected to be the top-down verification of DNA-predicted protein sequences, de novo sequencing, disulfide bond analysis and the combined top-down/bottom-up analysis of post-translational modifications.

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Year:  2004        PMID: 15102460     DOI: 10.1016/j.copbio.2003.12.002

Source DB:  PubMed          Journal:  Curr Opin Biotechnol        ISSN: 0958-1669            Impact factor:   9.740


  95 in total

1.  Topographic studies of the GroEL-GroES chaperonin complex by chemical cross-linking using diformyl ethynylbenzene: the power of high resolution electron transfer dissociation for determination of both peptide sequences and their attachment sites.

Authors:  Michael J Trnka; A L Burlingame
Journal:  Mol Cell Proteomics       Date:  2010-09-02       Impact factor: 5.911

2.  Improving software performance for peptide electron transfer dissociation data analysis by implementation of charge state- and sequence-dependent scoring.

Authors:  Peter R Baker; Katalin F Medzihradszky; Robert J Chalkley
Journal:  Mol Cell Proteomics       Date:  2010-05-31       Impact factor: 5.911

3.  Top-down tandem mass spectrometry on RNase A and B using a Qh/FT-ICR hybrid mass spectrometer.

Authors:  Sandrine Bourgoin-Voillard; Nancy Leymarie; Catherine E Costello
Journal:  Proteomics       Date:  2014-04-24       Impact factor: 3.984

4.  Electron capture dissociation of polypeptides in a three-dimensional quadrupole ion trap: Implementation and first results.

Authors:  Oleg A Silivra; Frank Kjeldsen; Igor A Ivonin; Roman A Zubarev
Journal:  J Am Soc Mass Spectrom       Date:  2005-01       Impact factor: 3.109

5.  Infrared multiphoton dissociation (IRMPD) and collisionally activated dissociation of peptides in a quadrupole ion trap with selective IRMPD of phosphopeptides.

Authors:  Matthew C Crowe; Jennifer S Brodbelt
Journal:  J Am Soc Mass Spectrom       Date:  2004-11       Impact factor: 3.109

6.  Side-chain fragmentation of alkylated cysteine residues in electron capture dissociation mass spectrometry.

Authors:  R J Chalkley; C S Brinkworth; A L Burlingame
Journal:  J Am Soc Mass Spectrom       Date:  2006-06-30       Impact factor: 3.109

7.  Formation of anionic peptide radicals in vacuo.

Authors:  Corey N W Lam; Ivan K Chu
Journal:  J Am Soc Mass Spectrom       Date:  2006-06-30       Impact factor: 3.109

8.  Fragmentation of oligoribonucleotides from gas-phase ion-electron reactions.

Authors:  Jiong Yang; Kristina Håkansson
Journal:  J Am Soc Mass Spectrom       Date:  2006-07-26       Impact factor: 3.109

9.  Supplemental activation method for high-efficiency electron-transfer dissociation of doubly protonated peptide precursors.

Authors:  Danielle L Swaney; Graeme C McAlister; Matthew Wirtala; Jae C Schwartz; John E P Syka; Joshua J Coon
Journal:  Anal Chem       Date:  2007-01-15       Impact factor: 6.986

10.  Characterization of 4-hydroxy-2-nonenal-modified peptides by liquid chromatography-tandem mass spectrometry using data-dependent acquisition: neutral loss-driven MS3 versus neutral loss-driven electron capture dissociation.

Authors:  Navin Rauniyar; Stanley M Stevens; Katalin Prokai-Tatrai; Laszlo Prokai
Journal:  Anal Chem       Date:  2009-01-15       Impact factor: 6.986

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