ArticleJournal of biomolecular NMR2009
Measuring 13Cbeta chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy.
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 28 papers.
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Who cites it
28 citing papers in PubMed.
- NMR methods for investigating functionally relevant biomolecular dynamics.Magnetic resonance letters · 2025Review
- Studying micro to millisecond protein dynamics using simple amideJournal of biomolecular NMR · 2023Article
- Cell-free synthesis of proteins with selectivelyMagnetic resonance (Gottingen, Germany) · 2023Article
- Conformational exchange of aromatic side chains byJournal of biomolecular NMR · 2018Article
- Late metabolic precursors for selective aromatic residue labeling.Journal of biomolecular NMR · 2018Review
- Measuring the signs of the methylJournal of biomolecular NMR · 2018Article
- Site-selectiveJournal of biomolecular NMR · 2017Article
- Measurement of protein backboneJournal of biomolecular NMR · 2017Article
- Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer.Journal of biomolecular NMR · 2017Review
- Site-selectiveJournal of biomolecular NMR · 2017Article
- (13)C-NMR studies on disulfide bond isomerization in bovine pancreatic trypsin inhibitor (BPTI).Journal of biomolecular NMR · 2016Article
- Fractional enrichment of proteins using [2-(13)C]-glycerol as the carbon source facilitates measurement of excited state 13Cα chemical shifts with improved sensitivity.Journal of biomolecular NMR · 2015Article
- Visualizing transient dark states by NMR spectroscopy.Quarterly reviews of biophysics · 2015Article
- An exact solution for R2,eff in CPMG experiments in the case of two site chemical exchange.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Off-resonance rotating-frame relaxation dispersion experiment for 13C in aromatic side chains using L-optimized TROSY-selection.Journal of biomolecular NMR · 2014Article
- Chemical exchange in biomacromolecules: past, present, and future.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Review
- Protein conformational exchange measured by 1H R1ρ relaxation dispersion of methyl groups.Journal of biomolecular NMR · 2013Article
- Specific 12CβD(2)12CγD(2)S13CεHD(2) isotopomer labeling of methionine to characterize protein dynamics by 1H and 13C NMR relaxation dispersion.Journal of the American Chemical Society · 2012Article
- Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected ¹³C CPMG relaxation dispersion.Journal of biomolecular NMR · 2012Article
- Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R(1ρ): an application to αB-crystallin.Journal of biomolecular NMR · 2012Article
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3 authors.
Funding
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Abstract
A labeling scheme is introduced that facilitates the measurement of accurate (13)C(beta) chemical shifts of invisible, excited states of proteins by relaxation dispersion NMR spectroscopy. The approach makes use of protein over-expression in a strain of E. coli in which the TCA cycle enzyme succinate dehydrogenase is knocked out, leading to the production of samples with high levels of (13)C enrichment (30-40%) at C(beta) side-chain carbon positions for 15 of the amino acids with little (13)C label at positions one bond removed (approximately 5%). A pair of samples are produced using [1-(13)C]-glucose/NaH(12)CO(3) or [2-(13)C]-glucose as carbon sources with isolated and enriched (>30%) (13)C(beta) positions for 11 and 4 residues, respectively. The efficacy of the labeling procedure is established by NMR spectroscopy. The utility of such samples for measurement of (13)C(beta) chemical shifts of invisible, excited states in exchange with visible, ground conformations is confirmed by relaxation dispersion studies of a protein-ligand binding exchange reaction in which the extracted chemical shift differences from dispersion profiles compare favorably with those obtained directly from measurements on ligand free and fully bound protein samples.
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