ArticleJournal of biomolecular NMR2011
Calculation of chemical shift anisotropy in proteins.
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 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 40 citations in OpenAlex.
- High-efficiency low-powerJournal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Molecular mechanisms and evolutionary robustness of a color switch in proteorhodopsins.Science advances · 2024Article
- Dynamic Coupling of Tyrosine 185 with the Bacteriorhodopsin Photocycle, as Revealed by Chemical Shifts, Assisted AF-QM/MM Calculations and Molecular Dynamic Simulations.International journal of molecular sciences · 2021Article
- Using quantum chemistry to estimate chemical shifts in biomolecules.Biophysical chemistry · 2020Review
- Accurate BackboneChemphyschem : a European journal of chemical physics and physical chemistry · 2020Article
- Determination of accurate backbone chemical shift tensors in microcrystalline proteins by integrating MAS NMR and QM/MM.Physical chemistry chemical physics : PCCP · 2018Article
- Enhanced NMR Discrimination of Pharmaceutically Relevant Molecular Crystal Forms through Fragment-Based Ab Initio Chemical Shift Predictions.Crystal growth & design · 2016Article
- Quantifying protein dynamics in the ps-ns time regime by NMR relaxation.Journal of biomolecular NMR · 2016Article
- Dynamic Water-Mediated Hydrogen Bonding in a Collagen Model Peptide.Biochemistry · 2015Article
- AFNMR: automated fragmentation quantum mechanical calculation of NMR chemical shifts for biomolecules.Journal of biomolecular NMR · 2015Article
- Coupling of Conformational Transitions in the N-terminal Domain of the 51-kDa FK506-binding Protein (FKBP51) Near Its Site of Interaction with the Steroid Receptor Proteins.The Journal of biological chemistry · 2015Article
- Correlation of chemical shifts predicted by molecular dynamics simulations for partially disordered proteins.Journal of biomolecular NMR · 2015Article
- 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
- Chemical shifts in biomolecules.Current opinion in structural biology · 2013Review
- Multidimensional magic angle spinning NMR spectroscopy for site-resolved measurement of proton chemical shift anisotropy in biological solids.Journal of the American Chemical Society · 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Individual peptide groups in proteins must exhibit some variation in the chemical shift anisotropy (CSA) of their constituent atoms, but not much is known about the extent or origins of this dispersion. Direct spectroscopic measurement of CSA remains technically challenging, and theoretical methods can help to overcome these limitations by estimating shielding tensors for arbitrary structures. Here we use an automated fragmentation quantum mechanics/molecular mechanics (AF-QM/MM) approach to compute (15)N, (13)C' and (1)H chemical shift tensors for human ubiquitin and the GB1 and GB3 fragments of staphylococcal protein G. The average and range of variation of the anisotropies is in good agreement with experimental estimates from solid-state NMR, and the variation among residues is somewhat smaller than that estimated from solution-state measurements. Hydrogen-bond effects account for much of the variation, both between helix and sheet regions, and within elements of secondary structure, but other effects (including variations in torsion angles) may play a role as well.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.