The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
A database of 660 peptide ion cross sections: Use of intrinsic size parameters for bona fide predictions of cross sections
Abstract
An ion trap/ion mobility/time-of-flight mass spectrometry technique has been used to measure collision cross sections for 660 peptide ions generated by tryptic digestion of 34 common proteins. Measured cross sections have been compiled into a database that contains peptide molecular weight and sequence information. The database is used to generate average intrinsic contributions to cross section (size parameters) for different amino acid residues by solving systems of equations that relate the unknown contributions of individual residues to the sequences and cross sections of database peptides. Size parameters are combined with information about amino acid composition to calculate cross sections for database peptides. Bona fide cross section predictions (made prior to measurement) for peptides observed in tryptic digests of sperm whale myoglobin and yeast enolase are made. Eight of 10 predicted cross sections are within 2% of the experimental values and all 10 are within 3.2%. The utility of size parameters for cross section prediction is explored and discussed.
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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
Ion/Ion Reactions in the Gas Phase: Proton Transfer Reactions Involving Multiply-Charged Proteins
Stephenson, J. L., & McLuckey, S. A. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9611755 · Cited by 215
Ion/Ion Proton Transfer Reactions for Protein Mixture Analysis
Stephenson, J. L., & McLuckey, S. A. (1996) · Analytical Chemistry · doi:10.1021/ac9605657 · Cited by 145
Cited by
Meier, F., Brunner, A.-D., Koch, S., Koch, H., Lubeck, M., Krause, M., Goedecke, N., Decker, J., Kosinski, T., Park, M. A., et al. (2018) · Molecular & Cellular Proteomics · doi:10.1074/mcp.tir118.000900 · Cited by 965
Recommendations for reporting ion mobility Mass Spectrometry measurements
Gabelica, V., Shvartsburg, A. A., Afonso, C., Barran, P., Benesch, J. L. P., Bleiholder, C., Bowers, M. T., Bilbao, A., Bush, M. F., Campbell, J. L., et al. (2019) · Mass Spectrometry Reviews · doi:10.1002/mas.21585 · Cited by 493
Self-citationIon mobility mass spectrometry of proteins and proteinassemblies
Uetrecht, C., Rose, R. J., van Duijn, E., Lorenzen, K., & Heck, A. J. R. (2010) · Chem. Soc. Rev. · doi:10.1039/b914002f · Cited by 462
High-field asymmetric waveform ion mobility spectrometry: A new tool for mass spectrometry
Guevremont, R. (2004) · Journal of Chromatography A · doi:10.1016/j.chroma.2004.08.119 · Cited by 444
Charge‐Induced Unzipping of Isolated Proteins to a Defined Secondary Structure
González Flórez, A. I., Mucha, E., Ahn, D., Gewinner, S., Schöllkopf, W., Pagel, K., & von Helden, G. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201510983 · Cited by 79
Metadata
- Authors
- Valentine, S. J., Counterman, A. E., & Clemmer, D. E.
- Venue
- Journal of the American Society for Mass Spectrometry
- Publisher
- American Chemical Society (ACS)
- Published
- 1999-11-01
- Volume
- 10
- Issue
- 11
- Pages
- 1188-1211
- ISSN
- 1044-0305 (ISSN-L)
- OpenAlex
- W1967287387
- Cited by
- 219
- References
- 3
- FWCI
- 4.26
- Type
- journal article
- Language
- en
- Open access
- closed
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- Valentine, S. J., Counterman, A. E., & Clemmer, D. E. (1999). A database of 660 peptide ion cross sections: Use of intrinsic size parameters for bona fide predictions of cross sections. Journal of the American Society for Mass Spectrometry. https://doi.org/10.1016/s1044-0305(99)00079-3
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