Electrospray Ionization Fourier Transform Mass Spectrometry of Macromolecules: The First Decade

Lorenz, Sarah A.; Maziarz, E. Peter; Wood, Troy D.

doi:10.1366/0003702991945209

Cited by 41 publications

(25 citation statements)

References 60 publications

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“…' Fenn's contribution was the development of electrospray ionization (ESI) (Fenn et al, 1989). The combination of ESI with Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) (Henry et al, 1989;Hendrickson & Emmett, 1999;Lorenz, Maziarz, & Wood, 1999) is a powerful tool for biomolecular analysis. ESI allows the analysis of ions of more than 100,000 Da in mass (Chen et al, 1995) while retaining optimum FT-ICR performance because of the typically observed low (below 4,000) mass-to-charge ratios.…”

Section: Introductionmentioning

confidence: 99%

The role of electron capture dissociation in biomolecular analysis

Cooper¹,

Håkansson²,

Marshall³

2004

Mass Spectrometry Reviews

473

472

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The introduction of electron capture dissociation (ECD) to electrospray (ESI) Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) constitutes a significant advance in the structural analysis of biomolecules. The fundamental features and benefits of ECD are discussed in this review. ECD is currently unique to FT-ICR MS and the fundamentals of that technique are outlined. The advantages and complementarity of ECD in relation to other tandem mass spectrometry (MS/MS) techniques, such as infrared multiphoton dissociation (IRMPD) and sustained off-resonance collision-induced dissociation (SORI-CID), are discussed. The instrumental considerations associated with implementation of ECD, including activated ion techniques and coupling to on-line separation techniques, are covered, as are the allied processes electronic excitation dissociation (EED), electron detachment dissociation (EDD), and hot electron capture (HECD). A major theme of this review is the role of ECD in proteomics, particularly for characterization of post-translational modifications (phosphorylation, glycosylation, carboxyglutamic acid, sulfation, acylation, and methionine oxidation) and the top-down approach to protein identification. The application of ECD to the analysis of polymers, peptide nucleic acids, and oligonucleotides is also discussed.

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Section: Introductionmentioning

confidence: 99%

The role of electron capture dissociation in biomolecular analysis

Cooper¹,

Håkansson²,

Marshall³

2004

Mass Spectrometry Reviews

473

472

View full text Add to dashboard Cite

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“…The electrospray source conditions can also influence the conformational distribution of the protein ions. These parameters include capillary temperature, source pressure and voltage [7,8].…”

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confidence: 99%

Electron capture dissociation distinguishes a single D-amino acid in a protein and probes the tertiary structure

Adams

Kjeldsen

Zubarev

et al. 2004

J. Am. Soc. Mass Spectrom.

120

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First results are reported on the application of ECD in analysis of 2ϩ and 3ϩ ions of stereoisomers of Trp-cage (NLYIQWLKDGGPSSGRPPPS), the smallest and fastest-folding protein, which exhibits a tightly folded tertiary structure in solution. The chiral recognition based on the ratios of the abundances of z 18 and z 19 fragments in ECD of 2ϩ ions was excellent even for a single amino acid (Tyr) D-substitution (R chiral ϭ 8.6). The chiral effect decreased with an increase of temperature at the electrospray ion source, as well as at a higher degree of ionization, 3ϩ ions (R chiral ϭ 1.5). A general approach is suggested for charge localization in nϩ ions by analysis of ECD mass spectra of (n ϩ 1)ϩ ions. Application of this approach to 3ϩ Trp-cage ions revealed the protonation probability order in 2ϩ ions: Arg 16 ӷ Gln 5 ϾϷ N-terminus. The ECD results for native form of the 2ϩ ions favor the preservation of the solution-phase tertiary structure, and chiral recognition through the interaction between the charges and the neutral bond network. Conversely, ECD of 3ϩ ions supports the dominance of ionic hydrogen bonding which determines a different gas-phase structure than found in solution. Vibrational activation of 2ϩ ions indicated greater stability of the native form, but the fragmentation patterns did not provide stereoisomer differentiation, thus underlying the special position of ECD among other MS/MS fragmentation techniques. Further ECD studies should yield more structural information as well as quantitative single-amino acid d/l content measurements in proteins. (J Am Soc Mass Spectrom 2004, 15, 1087-1098

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“…Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) [10] provides the highest mass resolution, highest mass resolving power, and highest mass accuracy (low ppm). When combined with electrospray ionization (ESI), FT-ICR MS [11,12] provides high analytical sensitivity requiring femtomoles or less of sample [13,14]. High resolution FT-ICR MS permits mass measurement of large peptides (>3000 Da) with a mass accuracy of a few ppm.…”

Section: Introductionmentioning

confidence: 99%