The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
SPARTA+: a modest improvement in empirical NMR chemical shift prediction by means of an artificial neural network
Open accessAbstract
NMR chemical shifts provide important local structural information for proteins and are key in recently described protein structure generation protocols. We describe a new chemical shift prediction program, SPARTA+, which is based on artificial neural networking. The neural network is trained on a large carefully pruned database, containing 580 proteins for which high-resolution X-ray structures and nearly complete backbone and 13Cβ chemical shifts are available. The neural network is trained to establish quantitative relations between chemical shifts and protein structures, including backbone and side-chain conformation, H-bonding, electric fields and ring-current effects. The trained neural network yields rapid chemical shift prediction for backbone and 13Cβ atoms, with standard deviations of 2.45, 1.09, 0.94, 1.14, 0.25 and 0.49 ppm for δ15N, δ13C’, δ13Cα, δ13Cβ, δ1Hα and δ1HN, respectively, between the SPARTA+ predicted and experimental shifts for a set of eleven validation proteins. These results represent a modest but consistent improvement (2–10%) over the best programs available to date, and appear to be approaching the limit at which empirical approaches can predict chemical shifts.
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Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
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 · cited 2×
“During protein structure calculations, chemical shift derived backbone //w torsion angles (Luginbühl et al. 1995; Cornilescu et al. 1999; Shen et al. 2009) are often used as empirical restraints, complementing the more traditional restraints derived from NOEs, J couplings and RDCs.”
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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
Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics
Granata, D., Camilloni, C., Vendruscolo, M., & Laio, A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218350110 · Cited by 143
Finding Our Way in the Dark Proteome
Bhowmick, A., Brookes, D. H., Yost, S. R., Dyson, H. J., Forman-Kay, J. D., Gunter, D., Head-Gordon, M., Hura, G. L., Pande, V. S., Wemmer, D. E., et al. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b06543 · Cited by 128
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Metadata
- Authors
- Shen, Y., & Bax, A.
- Venue
- Journal of Biomolecular NMR
- Published
- 2010-07-14
- Volume
- 48
- Issue
- 1
- Pages
- 13-22
- ISSN
- 0925-2738 (ISSN-L)
- 1573-5001
- OpenAlex
- W2100736103
- Cited by
- 552
- References
- 2
- FWCI
- 12.71
- Type
- journal article
- Language
- en
- Open access
- green
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