ArticleJournal of biomolecular NMR2011
Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Accurate ab initio prediction of NMR chemical shifts of nucleic acids and nucleic acids/protein complexes.Nucleic acids research · 2014Article
- Cytochrome-P450-cytochrome-b5 interaction in a membrane environment changes 15N chemical shift anisotropy tensors.The journal of physical chemistry. B · 2013Article
- NMR crystallography of enzyme active sites: probing chemically detailed, three-dimensional structure in tryptophan synthase.Accounts of chemical research · 2013Article
- Quantum chemical calculations of amide-15N chemical shift anisotropy tensors for a membrane-bound cytochrome-b5.The journal of physical chemistry. B · 2013Article
- Determination of 15N chemical shift anisotropy from a membrane-bound protein by NMR spectroscopy.The journal of physical chemistry. B · 2012Article
- Calculation of chemical shift anisotropy in proteins.Journal of biomolecular NMR · 2011Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
We performed density functional calculations of backbone (15)N shielding tensors in the regions of beta-sheet and turns of protein G. The calculations were carried out for all twenty-four beta-sheet residues and eight beta-turn residues in the protein GB3 and the results were compared with the available experimental data from solid-state and solution NMR measurements. Together with the alpha-helix data, our calculations cover 39 out of the 55 residues (or 71%) in GB3. The applicability of several computational models developed previously (Cai et al. in J Biomol NMR 45:245-253, 2009) to compute (15)N shielding tensors of alpha-helical residues is assessed. We show that the proposed quantum chemical computational model is capable of predicting isotropic (15)N chemical shifts for an entire protein that are in good correlation with experimental data. However, the individual components of the predicted (15)N shielding tensor agree with experiment less well: the computed values show much larger spread than the experimental data, and there is a profound difference in the behavior of the tensor components for alpha-helix/turns and beta-sheet residues. We discuss possible reasons for this.
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