ArticleJournal of biomolecular NMR2009
Density functional calculations of chemical shielding of backbone 15N in helical residues of protein G.
Article in Journal of biomolecular NMR, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 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
- Quantum chemical calculations of amide-15N chemical shift anisotropy tensors for a membrane-bound cytochrome-b5.The journal of physical chemistry. B · 2013Article
- Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic ¹⁵N chemical shielding anisotropy tensors.Journal of biomolecular NMR · 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
- Ultrahigh resolution protein structures using NMR chemical shift tensors.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G.Journal of biomolecular NMR · 2011Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
We performed density functional calculations of backbone (15)N chemical shielding tensors in selected helical residues of protein G. Here we describe a computationally efficient methodology to include most of the important effects in the calculation of chemical shieldings of backbone (15)N. We analyzed the role of long-range intra-protein electrostatic interactions by comparing models with different complexity in vacuum and in charge field. Our results show that the dipole moment of the alpha-helix can cause significant deshielding of (15)N; therefore, it needs to be considered when calculating (15)N chemical shielding. We found that it is important to include interactions with the side chains that are close in space when the charged form for ionizable side chains is adopted in the calculation. We also illustrate how the ionization state of these side chains can affect the chemical shielding tensor elements. Chemical shielding calculations using a 8-residue fragment model in vacuum and adopting the charged form of ionizable side chains yield a generally good agreement with experimental data.
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