Electron-capture dissociation tandem mass spectrometry

Current Opinion in Biotechnology

Volumn 15, Issue 1, 2004, Pages 12-16

  Zubarev, Roman A ^a  

^a UPPSALA UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ISOLEUCINE; LEUCINE; PEPTIDE; PROTEIN;

AMINO ACID SEQUENCE; ANALYTIC METHOD; COVALENT BOND; DISULFIDE BOND; DNA SEQUENCE; ELECTRON CAPTURE DISSOCIATION; ELECTRON TRANSPORT; FRAGMENTATION REACTION; HUMAN; ION CYCLOTRON RESONANCE MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN MODIFICATION; REVIEW; TANDEM MASS SPECTROMETRY;

EID: 1242351309     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2003.12.002     Document Type: Review

References (30)

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12. Palmblad M., Tsybin Y.O., Ramstrom M., Bergquist J., Hakansson P. Liquid chromatography and electron-capture dissociation in Fourier transform ion cyclotron resonance mass spectrometry. Rapid Commun. Mass Spectrom. 16:2002;988-992 The first successful attempt combining ECD on-line with LC/MS/ MS for the analysis of a standard peptide mixture and bovine serum albumin tryptic peptide digest. Meaningful sequence information, sufficient to identify the protein correctly with a Mascot search, was derived from each of the 13 most abundant peptide ions. The abstract also suggests (although the main text neither reports nor discusses) identification and localization of PTMs.
13. Tsybin Y.O., Håkansson P., Budnik B.A., Haselmann K.F., Kjeldsen F., Gorshkov M., Zubarev R.A. Improved low-energy electron injection systems for high rate electron capture dissociation in Fourier transform ion cyclotron resonance mass spectrometry. Rapid. Commun. Mass Spectrom. 15:2001;1849-1854.
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17. Zubarev R.A., Haselmann K.F., Budnik B.A., Kjeldsen F., Jensen F. Towards an understanding of the mechanism of electron capture dissociation: a historical perspective and modern ideas. Eur. J. Mass Spectrom. 8:2002;337-349.
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20. Ge Y., Lawhorn B.G., ElNaggar M., Strauss E., Park J.H., Begley T., McLafferty F.W. Top down characterization of larger proteins (45. kDa) by electron capture dissociation mass spectrometry J. Am. Chem. Soc. 124:2002;672-678 Several examples are given of the top-down, ECD-based approach to the characterization of errors in DNA-predicted protein sequences. In one example, the molecular weight of the 45 kDa phosphopantothenoylcysteine synthetase/decarboxylase (CoaBC), an enzyme involved in coenzyme A biosynthesis, was found to be 131 Da lower than that of the DNA prediction; the ECD spectrum showed that this was due to the removal of the N-terminal methionine residue.
21. Sze S.K., Ge Y., Oh H., McLafferty F.W. Plasma electron capture dissociation for the characterization of large proteins by top-down mass spectrometry. Anal. Chem. 75:2003;1599-1603.
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25. Kjeldsen F., Haselmann K.F., Budnik B.A., Sorensen E., Zubarev R.A. Complete characterization of post-translational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage. Anal. Chem. 75:2003;2355-2361 The REMMA procedure applied to the bovine milk PP3 protein containing 25% modifications by weight yielded all known modifications (five phosphorylations, two O- glycosylations and one N-glycosylation), as well as the previously unreported NeuNAc-Hex-[NeuNAc]HexNAc group O-linked to Ser60. It is argued that the approach can serve as a basis for high-throughput, high-sensitivity PTM characterization of biological important proteins.
26. α bond cleavage of the polypeptide chain without complete dissociation of the complex.
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30. Mann M., Jensen O.N. Proteomic analysis of post-translational modifications. Nat. Biotechnol. 21:2003;255-261 This recent review discusses the importance of high-sensitivity PTM analysis for providing insight into biological function. The potential of novel mass spectrometric peptide sequencing approaches, including ECD, for mapping modification sites is discussed. It is predicted that ECD in combination with novel hybrid FTICR instruments will provide characterization of labile modifications with a sensitivity and speed approaching standard mass-spectrometric peptide sequencing.