The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Hydrogen exchange mass spectrometry for the analysis of protein dynamics
Abstract
Hydrogen exchange coupled to mass spectrometry (MS) has become a valuable analytical tool for the study of protein dynamics. By combining information about protein dynamics with more classical functional data, a more thorough understanding of protein function can be obtained. In many cases, protein dynamics are directly related to specific protein functions such as conformational changes during enzyme activation or protein movements during binding. The method is made possible because labile backbone hydrogens in a protein will exchange with deuterium atoms when the protein is placed in a D 2 O solution. The subsequent increase in protein mass over time is measured with high‐resolution MS. The location of the deuterium incorporation is determined by monitoring deuterium incorporation in peptic fragments that are produced after the labeling reaction. In this review, we will summarize the general principles of the method, discuss the latest variations on the experimental protocol that probe different types of protein movements, and review other recent work and improvements in the field. © 2005 Wiley Periodicals, Inc.
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Cites
Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
Syka, J. E. P., Coon, J. J., Schroeder, M. J., Shabanowitz, J., & Hunt, D. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402700101 · Cited by 2,370
Docking Motif Interactions in MAP Kinases Revealed by Hydrogen Exchange Mass Spectrometry
Lee, T., Hoofnagle, A. N., Kabuyama, Y., Stroud, J., Min, X., Goldsmith, E. J., Chen, L., Resing, K. A., & Ahn, N. G. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00161-3 · Cited by 282 · cited 1×
“A study aimed at identifying regions in MAP kinases specific for binding two peptide docking motifs (DEJL and DEF) included the presentation of the distal effects of these ligand interactions (Lee et al., 2004).”
BackgroundLanman, J., Lam, T. T., Barnes, S., Sakalian, M., Emmett, M. R., Marshall, A. G., & Prevelige, P. E. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01245-7 · Cited by 206
Key interactions in HIV-1 maturation identified by hydrogen-deuterium exchange
Lanman, J., Lam, T. T., Emmett, M. R., Marshall, A. G., Sakalian, M., & Prevelige, P. E. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb790 · Cited by 164
Tuma, R., Coward, L. U., Kirk, M. C., Barnes, S., & Prevelige, P. E. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4383 · Cited by 53
Cited by
An NMR Perspective on Enzyme Dynamics
Boehr, D. D., Dyson, H. J., & Wright, P. E. (2006) · Chemical Reviews · doi:10.1021/cr050312q · Cited by 458
Tracking heavy water (D 2 O) incorporation for identifying and sorting active microbial cells
Berry, D., Mader, E., Lee, T. K., Woebken, D., Wang, Y., Zhu, D., Palatinszky, M., Schintlmeister, A., Schmid, M. C., Hanson, B. T., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420406112 · Cited by 455
Mechanism-based corrector combination restores ΔF508-CFTR folding and function
Okiyoneda, T., Veit, G., Dekkers, J. F., Bagdany, M., Soya, N., Xu, H., Roldan, A., Verkman, A. S., Kurth, M., Simon, A., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1253 · Cited by 378
Force interacts with macromolecular structure in activation of TGF-β
Dong, X., Zhao, B., Iacob, R. E., Zhu, J., Koksal, A. C., Lu, C., Engen, J. R., & Springer, T. A. (2017) · Nature · doi:10.1038/nature21035 · Cited by 273
Self-citationMartin, C. J., Datta, A., Littlefield, C., Kalra, A., Chapron, C., Wawersik, S., Dagbay, K. B., Brueckner, C. T., Nikiforov, A., Danehy, F. T., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aay8456 · Cited by 224
Metadata
- Authors
- Wales, T. E., & Engen, J. R.
- Venue
- Mass Spectrometry Reviews
- Publisher
- Wiley
- Published
- 2005-10-05
- Volume
- 25
- Issue
- 1
- Pages
- 158-170
- ISSN
- 0277-7037 (ISSN-L)
- 1098-2787
- OpenAlex
- W2147024375
- Cited by
- 862
- References
- 5
- FWCI
- 15.90
- Type
- journal article
- Language
- en
- Open access
- closed
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