ArticleJournal of the American Chemical Society2008
Dependence of amino acid side chain 13C shifts on dihedral angle: application to conformational analysis.
Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 78 citations in OpenAlex.
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- Structural basis of substrate recognition and allosteric activation of the proapoptotic mitochondrial HtrA2 protease.Nature communications · 2024Article
- Profiling Enzyme Activity of l-Asparaginase II by NMR-Based Methyl Fingerprinting at Natural Abundance.Journal of the American Chemical Society · 2023Article
- Conformational selection guides β-arrestin recruitment at a biased G protein-coupled receptor.Science (New York, N.Y.) · 2022Article
- Targeting the cryptic sites: NMR-based strategy to improve protein druggability by controlling the conformational equilibrium.Science advances · 2020Article
- Determining isoleucine side-chain rotamer-sampling in proteins fromChemical communications (Cambridge, England) · 2019Article
- GPCR drug discovery: integrating solution NMR data with crystal and cryo-EM structures.Nature reviews. Drug discovery · 2019Review
- Solution NMR spectroscopy of GPCRs: Residue-specific labeling strategies with a focus onMethods in cell biology · 2019Article
- Transitions in DNA polymerase β μs-ms dynamics related to substrate binding and catalysis.Nucleic acids research · 2018Article
- Phosphorylation-induced conformation of βNature communications · 2018Article
- Recent developments in solution nuclear magnetic resonance (NMR)-based molecular biology.Journal of molecular medicine (Berlin, Germany) · 2018Review
- Pressure dependence of side chainJournal of biomolecular NMR · 2017Article
- Article
- Dynamic regulation of GDP binding to G proteins revealed by magnetic field-dependent NMR relaxation analyses.Nature communications · 2017Article
- Metal Ion Binding at the Catalytic Site Induces Widely Distributed Changes in a Sequence Specific Protein-DNA Complex.Biochemistry · 2016Article
- NMR Methods to Study Dynamic Allostery.PLoS computational biology · 2016Review
- Side Chain Conformational Distributions of a Small Protein Derived from Model-Free Analysis of a Large Set of Residual Dipolar Couplings.Journal of the American Chemical Society · 2015Article
- Dynamic multidrug recognition by multidrug transcriptional repressor LmrR.Scientific reports · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Chemical shift data from the BiomagResDataBank and conformational data derived from the protein data bank have been correlated in order to explore the conformational dependence of side chain (13)C resonance shifts. Consistent with predictions based on steric compression, upfield shifts for Cgamma resonances of Thr, Val, Ile, Leu, Met, Arg, Lys, Glu, and Gln residues correlate with both the number of heavy atom (nonproton) gamma-substituents and with gauche conformational orientations of gamma-substituents. The (13)C shift/conformation correlations are most apparent for Cgamma carbons but also can be observed at positions further from the backbone. Intraresidue steric conflict leads to a correlation between upfield-shifted side chain (13)C resonances and statistically lower probabilities in surveys of protein side chain conformation. Illustrative applications to the DNA pol lambda lyase domain and to dihydrofolate reductase are discussed. In the latter case, (13)C shift analysis indicates that the conformation of the remote residue V119 on the betaF-betaG loop is correlated with the redox state of the bound pyridine nucleotide cofactor, providing one basis for discrimination between substrate and product. It is anticipated that (13)C shift data for protein sidechains can provide a useful basis for the analysis of conformational changes even in large, deuterated proteins. Additionally, the large dependence of the leucine methyl shift difference, deltaCdelta1-deltaCdelta2, on both chi1 and chi2 is sufficient to allow this parameter to be used as a restraint in structure calculations if stereospecific assignment data are available.
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