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NMR Structure Determination for Larger Proteins Using Backbone-Only Data
Open accessAbstract
Examining the Backbone: Determination of tertiary protein structures by nuclear magnetic resonance (NMR) currently relies heavily on side-chain NMR data. The assignment of side-chain atoms is challenging. In addition, proteins larger than 15 kilodaltons (kD) must be deuterated to improve resolution and this eliminates the possibility of measuring long-range interproton distance constraints. Now Raman et al. (p. 1014 , published online 4 February) use backbone-only NMR data—chemical shifts, residual dipolar coupling, and backbone amide proton distances—available from highly deuterated proteins to guide conformational searching in the Rosetta structure prediction protocol. Using this new protocol, they were able to generate accurate structures for proteins of up to 25 kD.
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Cites
LGA: a method for finding 3D similarities in protein structures
Zemla, A. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg571 · Cited by 1,069
Cited by
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Marks, D. S., Colwell, L. J., Sheridan, R., Hopf, T. A., Pagnani, A., Zecchina, R., & Sander, C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028766 · Cited by 1,144
Macromolecular modeling and design in Rosetta: recent methods and frameworks
Leman, J. K., Weitzner, B. D., Lewis, S. M., Adolf-Bryfogle, J., Alam, N., Alford, R. F., Aprahamian, M., Baker, D., Barlow, K. A., Barth, P., et al. (2020) · Nature Methods · doi:10.1038/s41592-020-0848-2 · Cited by 888
Self-citationProtein structure prediction from sequence variation
Marks, D. S., Hopf, T. A., & Sander, C. (2012) · Nature Biotechnology · doi:10.1038/nbt.2419 · Cited by 622
A protein fold switch joins the circadian oscillator to clock output in cyanobacteria
Chang, Y.-G., Cohen, S. E., Phong, C., Myers, W. K., Kim, Y.-I., Tseng, R., Lin, J., Zhang, L., Boyd, J. S., Lee, Y., et al. (2015) · Science · doi:10.1126/science.1260031 · Cited by 212
Integrative structure modeling of macromolecular assemblies from proteomics data
Lasker, K., Phillips, J. L., Russel, D., Velázquez-Muriel, J., Schneidman-Duhovny, D., Tjioe, E., Webb, B., Schlessinger, A., & Sali, A. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r110.000067 · Cited by 71
Metadata
- Authors
- Raman, S., Lange, O. F., Rossi, P., Tyka, M., Wang, X., Aramini, J., Liu, G., Ramelot, T. A., Eletsky, A., Szyperski, T., Kennedy, M. A., Prestegard, J., Montelione, G. T., & Baker, D.
- Venue
- Science
- Published
- 2010-02-19
- Volume
- 327
- Issue
- 5968
- Pages
- 1014-1018
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2092024874
- Cited by
- 268
- References
- 1
- FWCI
- 14.18
- Type
- journal article
- Language
- en
- Open access
- green
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- Raman, S., Lange, O. F., Rossi, P., Tyka, M., Wang, X., Aramini, J., Liu, G., Ramelot, T. A., Eletsky, A., Szyperski, T., Kennedy, M. A., Prestegard, J., Montelione, G. T., & Baker, D. (2010). NMR Structure Determination for Larger Proteins Using Backbone-Only Data. Science. https://doi.org/10.1126/science.1183649
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