The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
NMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination
Open accessAbstract
In this tutorial review, we discuss the utilization of chemical shift information as well as ab initio calculations of nuclear shieldings for protein structure determination. Both the empirical and computational aspects of the chemical shift are reviewed and the role of molecular dynamics and the accuracy of different computational methods are discussed. It is anticipated that incorporating theoretical information on chemical shifts will increase the accuracy of protein structures, in the solid and liquid state alike, and extend the applicability of NMR spectroscopy to ever larger systems.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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 by
Lodewyk, M. W., Siebert, M. R., & Tantillo, D. J. (2012) · Chemical Reviews · doi:10.1021/cr200106v · Cited by 1,287
An introduction to NMR-based approaches for measuring protein dynamics
Kleckner, I. R., & Foster, M. P. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.10.012 · Cited by 561
Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Sequence-Specific Random Coil Chemical Shifts of Intrinsically Disordered Proteins
Tamiola, K., Acar, B., & Mulder, F. A. A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja105656t · Cited by 326
Self-citationInterpreting protein chemical shift data
Wishart, D. S. (2011) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2010.07.004 · Cited by 252
Metadata
- Authors
- Mulder, F. A. A., & Filatov, M.
- Venue
- Chem. Soc. Rev.
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2010
- Volume
- 39
- Issue
- 2
- Pages
- 578-590
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2157530469
- Cited by
- 216
- References
- 1
- FWCI
- 0.70
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: NMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination. https://app.cochat.ai/papers/10.1039/b811366c
- The paper
- Mulder, F. A. A., & Filatov, M. (2010). NMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination. Chem. Soc. Rev. https://doi.org/10.1039/b811366c
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
