The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Infrared Multiphoton Dissociation of Large Multiply Charged Ions for Biomolecule Sequencing
Abstract
Characterization and verification of the structures of large biomolecules with high-resolution tandem Fourier transform mass spectrometry with electrospray ionization is critically dependent on the technique used to fragment the multiply charged ions produced. Infrared multiphoton dissociation (IRMPD) of ionized proteins as large as carbonic anhydrase (29 kDa) yields fragment information similar to, but with valuable additions to, that of other dissociation techniques. IRMPD yields product ions on-axis, providing efficient dissociation in further stages; MS3 of ubiquitin (8.6 kDa) yields 11 new sequence ions. Optimum irradiation times for protein ion dissociation vary by more than a factor of 6, with times for oligonucleotides far lower, possibly due to photon resonance with a P-O stretching frequency. IRMPD provides far greater selectivity than collisionally activated dissociation and also appears to yield much less mass discrimination and to dissociate much more stable ions. A technique to remove product ions on formation from the laser beam should improve the present efficiencies of 30-80%.
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Cites
Electrospray Ionization for Mass Spectrometry of Large Biomolecules
Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., & Whitehouse, C. M. (1989) · Science · doi:10.1126/science.2675315 · Cited by 7,634
Cited by
Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process
Zubarev, R. A., Kelleher, N. L., & McLafferty, F. W. (1998) · Journal of the American Chemical Society · doi:10.1021/ja973478k · Cited by 1,881
Self-citationOligosaccharide Analysis by Mass Spectrometry: A Review of Recent Developments
Kailemia, M. J., Ruhaak, L. R., Lebrilla, C. B., & Amster, I. J. (2014) · Analytical Chemistry · doi:10.1021/ac403969n · Cited by 377
Complete Protein Characterization Using Top-Down Mass Spectrometry and Ultraviolet Photodissociation
Shaw, J. B., Li, W., Holden, D. D., Zhang, Y., Griep-Raming, J., Fellers, R. T., Early, B. P., Thomas, P. M., Kelleher, N. L., & Brodbelt, J. S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4029654 · Cited by 371
Extending Top-Down Mass Spectrometry to Proteins with Masses Greater Than 200 Kilodaltons
Han, X., Jin, M., Breuker, K., & McLafferty, F. W. (2006) · Science · doi:10.1126/science.1128868 · Cited by 328
Self-citationProcessing Complex Mixtures of Intact Proteins for Direct Analysis by Mass Spectrometry
Meng, F., Cargile, B. J., Patrie, S. M., Johnson, J. R., McLoughlin, S. M., & Kelleher, N. L. (2002) · Analytical Chemistry · doi:10.1021/ac020049i · Cited by 183
Metadata
- Authors
- Little, D. P., Speir, J. P., Senko, M. W., O'Connor, P. B., & McLafferty, F. W.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1994-09-15
- Volume
- 66
- Issue
- 18
- Pages
- 2809-2815
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W2083991421
- Cited by
- 753
- References
- 1
- FWCI
- 13.21
- Type
- journal article
- Language
- en
- Open access
- closed
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- Little, D. P., Speir, J. P., Senko, M. W., O'Connor, P. B., & McLafferty, F. W. (1994). Infrared Multiphoton Dissociation of Large Multiply Charged Ions for Biomolecule Sequencing. Analytical Chemistry. https://doi.org/10.1021/ac00090a004
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