ArticleJournal of biomolecular NMR2012
On the calculation of ³Jαβ-coupling constants for side chains in proteins.
Article in Journal of biomolecular NMR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- On the Validation of Protein Force Fields Based on Structural Criteria.The journal of physical chemistry. B · 2024Article
- Analysis of chi angle distributions in free amino acids via multiplet fitting of proton scalar couplings.Magnetic resonance (Gottingen, Germany) · 2024Article
- On the Use of Side-Chain NMR Relaxation Data to Derive Structural and Dynamical Information on Proteins: A Case Study Using Hen Lysozyme.Chembiochem : a European journal of chemical biology · 2021Article
- On the use ofJournal of biomolecular NMR · 2021Article
- Force field-dependent solution properties of glycine oligomers.Journal of computational chemistry · 2015Article
- On the use of one-step perturbation to investigate the dependence of NOE-derived atom-atom distance bound violations of peptides upon a variation of force-field parameters.European biophysics journal : EBJ · 2014Article
- Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data.Biophysical reviews · 2012Review
- Solvating atomic level fine-grained proteins in supra-molecular level coarse-grained water for molecular dynamics simulations.European biophysics journal : EBJ · 2012Article
- An improved structural characterisation of reduced French bean plastocyanin based on NMR data and local-elevation molecular dynamics simulation.European biophysics journal : EBJ · 2012Article
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Authors and funding
4 authors.
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Abstract
Structural knowledge about proteins is mainly derived from values of observables, measurable in NMR spectroscopic or X-ray diffraction experiments, i.e. absorbed or scattered intensities, through theoretically derived relationships between structural quantities such as atom positions or torsional angles on the one hand and observable quantities such as squared structure factor amplitudes, NOE intensities or (3) J-coupling constants on the other. The standardly used relation connecting (3) J-couplings to torsional angles is the Karplus relation, which is used in protein structure refinement as well as in the evaluation of simulated properties of proteins. The accuracy of the simple and generalised Karplus relations is investigated using side-chain structural and (3) J (αβ)-coupling data for three different proteins, Plastocyanin, Lysozyme, and FKBP, for which such data are available. The results show that the widely used Karplus relations are only a rough estimate for the relation between (3) J (αβ)-couplings and the corresponding χ(1)-angle in proteins.
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