The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Protein structure determination from NMR chemical shifts
Open accessAbstract
NMR spectroscopy plays a major role in the determination of the structures and dynamics of proteins and other biological macromolecules. Chemical shifts are the most readily and accurately measurable NMR parameters, and they reflect with great specificity the conformations of native and nonnative states of proteins. We show, using 11 examples of proteins representative of the major structural classes and containing up to 123 residues, that it is possible to use chemical shifts as structural restraints in combination with a conventional molecular mechanics force field to determine the conformations of proteins at a resolution of 2 Å or better. This strategy should be widely applicable and, subject to further development, will enable quantitative structural analysis to be carried out to address a range of complex biological problems not accessible to current structural techniques.
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Cites
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical Information
Dominguez, C., Boelens, R., & Bonvin, A. M. J. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja026939x · Cited by 3,187
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957
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Progress in Modeling of Protein Structures and Interactions.
Schueler-Furman, O., Wang, C., Bradley, P., Misura, K., & Baker, D. (2005) · Science · doi:10.1126/science.1112160 · Cited by 294
Cited by
The role of dynamic conformational ensembles in biomolecular recognition
Boehr, D. D., Nussinov, R., & Wright, P. E. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.232 · Cited by 2,008
The ensemble nature of allostery
Motlagh, H. N., Wrabl, J. O., Li, J., & Hilser, V. J. (2014) · Nature · doi:10.1038/nature13001 · Cited by 1,247
Consistent blind protein structure generation from NMR chemical shift data
Shen, Y., Lange, O., Delaglio, F., Rossi, P., Aramini, J. M., Liu, G., Eletsky, A., Wu, Y., Singarapu, K. K., Lemak, A., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800256105 · Cited by 855
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Controlling Allosteric Networks in Proteins
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Metadata
- Authors
- Cavalli, A., Salvatella, X., Dobson, C. M., & Vendruscolo, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2007-06-05
- Volume
- 104
- Issue
- 23
- Pages
- 9615-9620
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1978545297
- Cited by
- 561
- References
- 5
- FWCI
- 16.52
- Type
- journal article
- Language
- en
- Open access
- green
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- Cavalli, A., Salvatella, X., Dobson, C. M., & Vendruscolo, M. (2007). Protein structure determination from NMR chemical shifts. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0610313104
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