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Secondary and Tertiary Structural Effects on Protein NMR Chemical Shifts: an ab Initio Approach
Abstract
Recent theoretical developments permit the prediction of 1 H, 13 C, 15 N, and 19 F nuclear magnetic resonance chemical shifts in proteins and offer new ways of analyzing secondary and tertiary structure as well as for probing protein electrostatics. For 13 C, φ, ψ torsion angles dominate shielding for Cα and Cβ, but the addition of hydrogen bonding and electrostatics gives even better accord with experiment. For 15 N H , side chain (χ 1 ) torsion angles are also important, as are nearest neighbor sequence effects, whereas for 1 H N , hydrogen bonding is particularly significant. For 19 F, weak or long-range electrostatic fields dominate 19 F shielding nonequivalencies. The ability to predict chemical shifts in proteins from known or test structures opens new avenues to structure refinement or determination, especially for condensed systems.
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Cited by
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
Shen, Y., & Bax, A. (2007) · Journal of Biomolecular NMR · doi:10.1007/s10858-007-9166-6 · Cited by 359
Structural adaptation of fungal cell wall in hypersaline environment
Fernando, L. D., Pérez-Llano, Y., Dickwella Widanage, M. C., Jacob, A., Martínez-Ávila, L., Lipton, A. S., Gunde-Cimerman, N., Latgé, J.-P., Batista-García, R. A., & Wang, T. (2023) · Nature Communications · doi:10.1038/s41467-023-42693-6 · Cited by 91
Metadata
- Authors
- de Dios, A. C., Pearson, J. G., & Oldfield, E.
- Venue
- Science
- Published
- 1993-06-04
- Volume
- 260
- Issue
- 5113
- Pages
- 1491-1496
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1992933392
- Cited by
- 444
- References
- 0
- FWCI
- 20.53
- Type
- journal article
- Language
- en
- Open access
- closed
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- de Dios, A. C., Pearson, J. G., & Oldfield, E. (1993). Secondary and Tertiary Structural Effects on Protein NMR Chemical Shifts: an ab Initio Approach. Science. https://doi.org/10.1126/science.8502992
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