The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry
Open accessAbstract
We have used intramolecular cross-linking, MS, and sequence threading to rapidly identify the fold of a model protein, bovine basic fibroblast growth factor (FGF)-2. Its tertiary structure was probed with a lysine-specific cross-linking agent, bis(sulfosuccinimidyl) suberate (BS 3 ). Sites of cross-linking were determined by tryptic peptide mapping by using time-of-flight MS. Eighteen unique intramolecular lysine (Lys-Lys) cross-links were identified. The assignments for eight cross-linked peptides were confirmed by using post source decay MS. The interatomic distance constraints were all consistent with the tertiary structure of FGF-2. These relatively few constraints, in conjunction with threading, correctly identified FGF-2 as a member of the β-trefoil fold family. To further demonstrate utility, we used the top-scoring homolog, IL-1β, to build an FGF-2 homology model with a backbone error of 4.8 Å (rms deviation). This method is fast, is general, uses small amounts of material, and is amenable to automation.
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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
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984
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False discovery rate estimation for cross-linked peptides identified by mass spectrometry
Walzthoeni, T., Claassen, M., Leitner, A., Herzog, F., Bohn, S., Förster, F., Beck, M., & Aebersold, R. (2012) · Nature Methods · doi:10.1038/nmeth.2103 · Cited by 301
The diverse and expanding role of mass spectrometry in structural and molecular biology
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Walzthoeni, T., Leitner, A., Stengel, F., & Aebersold, R. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.02.008 · Cited by 146
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Holding, A. N. (2015) · Methods · doi:10.1016/j.ymeth.2015.06.010 · Cited by 107
Metadata
- Authors
- Young, M. M., Tang, N., Hempel, J. C., Oshiro, C. M., Taylor, E. W., Kuntz, I. D., Gibson, B. W., & Dollinger, G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-05-16
- Volume
- 97
- Issue
- 11
- Pages
- 5802-5806
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2012534919
- Cited by
- 459
- References
- 2
- FWCI
- 4.84
- Type
- journal article
- Language
- en
- Open access
- green
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- Young, M. M., Tang, N., Hempel, J. C., Oshiro, C. M., Taylor, E. W., Kuntz, I. D., Gibson, B. W., & Dollinger, G. (2000). High throughput protein fold identification by using experimental constraints derived from intramolecular cross-links and mass spectrometry. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.090099097
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