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Mapping Protein−Protein Interactions in Solution by NMR Spectroscopy
Abstract
NMR is very well suited to the study of especially weak protein-protein interactions, as no crystallization is required. The available NMR methods to this end are reviewed and illustrated with applications from the recent biochemical literature: intermolecular NOEs, cross-saturation, chemical shift perturbation, dynamics and exchange perturbation, paramagnetic methods, and dipolar orientation. Most of these methods are now routinely applied for complexes with total molecular mass of 60 kDa and can likely be applied to systems up to 1000 kDa. A substantial fraction of complexes studied show distinct effects of induced fit affecting structural and dynamical properties beyond the contact interface.
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Cited by
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Dominguez, C., Boelens, R., & Bonvin, A. M. J. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja026939x · Cited by 3,187
Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex
Brzovic, P. S., Keeffe, J. R., Nishikawa, H., Miyamoto, K., Fox, D., Fukuda, M., Ohta, T., & Klevit, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0836054100 · Cited by 346
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
Karagöz, G. E., Duarte, A. M. S., Akoury, E., Ippel, H., Biernat, J., Morán Luengo, T., Radli, M., Didenko, T., Nordhues, B. A., Veprintsev, D. B., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.037 · Cited by 318
“…caused by the combined effects of (1) the increase in molecular weight upon complex formation, which increases transverse relaxation rates and thereby line width, and (2) the chemical exchange at the contact surface (Dekker et al., 1993; Sette et al., 1997; Wüthrich, 2003; Zuiderweg, 2002).”
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Xie, J., Reverdatto, S., Frolov, A., Hoffmann, R., Burz, D. S., & Shekhtman, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801622200 · Cited by 252
Integrating diverse data for structure determination of macromolecular assemblies
Alber, F., Förster, F., Korkin, D., Topf, M., & Sali, A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.060407.135530 · Cited by 206
Metadata
- Authors
- Zuiderweg, E. R. P.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2001-12-05
- Volume
- 41
- Issue
- 1
- Pages
- 1-7
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2157566126
- Cited by
- 534
- References
- 0
- FWCI
- 11.56
- Type
- journal article
- Language
- en
- Open access
- closed
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- Zuiderweg, E. R. P. (2002). Mapping Protein−Protein Interactions in Solution by NMR Spectroscopy. Biochemistry. https://doi.org/10.1021/bi011870b
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