The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Stepwise evolution of protein native structure with electrospray into the gas phase, 10 −12 to 10 2 s
Open accessAbstract
Mass spectrometry (MS) has been revolutionized by electrospray ionization (ESI), which is sufficiently “gentle” to introduce nonvolatile biomolecules such as proteins and nucleic acids (RNA or DNA) into the gas phase without breaking covalent bonds. Although in some cases noncovalent bonding can be maintained sufficiently for ESI/MS characterization of the solution structure of large protein complexes and native enzyme/substrate binding, the new gaseous environment can ultimately cause dramatic structural alterations. The temporal (picoseconds to minutes) evolution of native protein structure during and after transfer into the gas phase, as proposed here based on a variety of studies, can involve side-chain collapse, unfolding, and refolding into new, non-native structures. Control of individual experimental factors allows optimization for specific research objectives.
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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
Matrix-assisted ultraviolet laser desorption of non-volatile compounds
Karas, M., Bachmann, D., Bahr, U., & Hillenkamp, F. (1987) · International Journal of Mass Spectrometry and Ion Processes · doi:10.1016/0168-1176(87)87041-6 · Cited by 1,953
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-citationStudying noncovalent protein complexes by electrospray ionization mass spectrometry
Loo, J. A. (1997) · Mass Spectrometry Reviews · doi:10.1002/(sici)1098-2787(1997)16:1<1::aid-mas1>3.0.co;2-l · Cited by 1,182
Investigation of intact protein complexes by mass spectrometry
Heck, A. J. R., & van den Heuvel, R. H. H. (2004) · Mass Spectrometry Reviews · doi:10.1002/mas.10081 · Cited by 583
Detection of noncovalent receptor-ligand complexes by mass spectrometry
Ganem, B., Li, Y. T., & Henion, J. D. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00016a069 · Cited by 506
Daniel, J. M., Friess, S. D., Rajagopalan, S., Wendt, S., & Zenobi, R. (2002) · International Journal of Mass Spectrometry · doi:10.1016/s1387-3806(02)00585-7 · Cited by 475
Katta, V., & Chait, B. T. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00022a058 · Cited by 475
Precision proteomics: The case for high resolution and high mass accuracy
Mann, M., & Kelleher, N. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800788105 · Cited by 450
Micelles Protect Membrane Complexes from Solution to Vacuum
Barrera, N. P., Di Bartolo, N., Booth, P. J., & Robinson, C. V. (2008) · Science · doi:10.1126/science.1159292 · Cited by 360
Cited by
Lanucara, F., Holman, S. W., Gray, C. J., & Eyers, C. E. (2014) · Nature Chemistry · doi:10.1038/nchem.1889 · Cited by 901
Top‐down proteomics in health and disease: Challenges and opportunities
Gregorich, Z. R., & Ge, Y. (2014) · PROTEOMICS · doi:10.1002/pmic.201300432 · Cited by 217
Belov, M. E., Damoc, E., Denisov, E., Compton, P. D., Horning, S., Makarov, A. A., & Kelleher, N. L. (2013) · Analytical Chemistry · doi:10.1021/ac4029328 · Cited by 175
Advances in the Mass Spectrometry of Membrane Proteins: From Individual Proteins to Intact Complexes
Barrera, N. P., & Robinson, C. V. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062309-093307 · Cited by 154
Zhou, M., Lantz, C., Brown, K. A., Ge, Y., Paša-Tolić, L., Loo, J. A., & Lermyte, F. (2020) · Chemical Science · doi:10.1039/d0sc04392c · Cited by 146
Metadata
- Authors
- Breuker, K., & McLafferty, F. W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-11-25
- Volume
- 105
- Issue
- 47
- Pages
- 18145-18152
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2169873068
- Cited by
- 423
- References
- 49
- FWCI
- 7.47
- Type
- journal article
- Language
- en
- Open access
- green
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- Breuker, K., & McLafferty, F. W. (2008). Stepwise evolution of protein native structure with electrospray into the gas phase, 10 −12 to 10 2 s. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0807005105
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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