ArticleJournal of biomolecular NMR1997
Protein phi and psi dihedral restraints determined from multidimensional hypersurface correlations of backbone chemical shifts and their use in the determination of protein tertiary structures.
Article in Journal of biomolecular NMR, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Structural characterization of KKT4, an unconventional microtubule-binding kinetochore protein.Structure (London, England : 1993) · 2021Article
- Predicting the redox state and secondary structure of cysteine residues using multi-dimensional classification analysis of NMR chemical shifts.Journal of biomolecular NMR · 2016Article
- Type I and II β-turns prediction using NMR chemical shifts.Journal of biomolecular NMR · 2014Article
- Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- The predictive accuracy of secondary chemical shifts is more affected by protein secondary structure than solvent environment.Journal of biomolecular NMR · 2010Article
- Empirical isotropic chemical shift surfaces.Journal of biomolecular NMR · 2007Article
- Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology.Journal of biomolecular NMR · 2007Article
- A new model for chemical shifts of amide hydrogens in proteins.Journal of biomolecular NMR · 2007Article
- A Bayesian-probability-based method for assigning protein backbone dihedral angles based on chemical shifts and local sequences.Journal of biomolecular NMR · 2007Article
- Structural analysis of nanoscale self-assembled discoidal lipid bilayers by solid-state NMR spectroscopy.Biophysical journal · 2006Article
- PREDITOR: a web server for predicting protein torsion angle restraints.Nucleic acids research · 2006Article
- Secondary structural effects on protein NMR chemical shifts.Journal of biomolecular NMR · 2004Article
- Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts.Journal of biomolecular NMR · 2003Article
- RefDB: a database of uniformly referenced protein chemical shifts.Journal of biomolecular NMR · 2003Article
- Determination of protein global folds using backbone residual dipolar coupling and long-range NOE restraints.Journal of biomolecular NMR · 2003Article
- Combining NMR spectral and structural data to form models of polychlorinated dibenzodioxins, dibenzofurans, and biphenyls binding to the AhR.Journal of computer-aided molecular design · 2002Article
- Developing 13C NMR quantitative spectrometric data-activity relationship (QSDAR) models of steroid binding to the corticosteroid binding globulin.Journal of computer-aided molecular design · 2001Article
- 13C(alpha) and 13C(beta) chemical shifts as a tool to delineate beta-hairpin structures in peptides.Journal of biomolecular NMR · 2001Article
- C alpha and C beta carbon-13 chemical shifts in proteins from an empirical database.Journal of biomolecular NMR · 1999Article
- Protein backbone angle restraints from searching a database for chemical shift and sequence homology.Journal of biomolecular NMR · 1999Article
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Authors and funding
2 authors.
Funding
Abstract
The chemical shifts of the backbone atoms of proteins can be used to obtain restraints that can be incorporated into structure determination methods. Each chemical shift can be used to define a restraint and these restraints can be simultaneously used to define the local, secondary structure features. The global fold can be determined by a combined use of the chemical shift based restraints along with the long-range information present in the NOEs of partially deuterated proteins or the amide-amide NOEs but not from such limited NOE data sets alone. This approach has been demonstrated to be capable of determining the overall folding pattern of four proteins. This suggests that solution-state NMR methods can be extended to the structure determination of larger proteins by using the information present in the chemical shifts of the backbone atoms along with the data that can be obtained on a small number of labeled forms.
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