ArticleJournal of biomolecular NMR2003
A novel strategy for the assignment of side-chain resonances in completely deuterated large proteins using 13C spectroscopy.
Article in Journal of biomolecular NMR, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 93 citations in OpenAlex.
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- Driving force of biomolecular liquid-liquid phase separation probed by nuclear magnetic resonance spectroscopy.Biophysics reports · 2022Article
- A methyl-TROSY approach for NMR studies of high-molecular-weight DNA with application to the nucleosome core particle.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins.Journal of biomolecular NMR · 2019Article
- Direct ¹³C-detected NMR experiments for mapping and characterization of hydrogen bonds in RNA.Journal of biomolecular NMR · 2016Article
- Paramagnetic relaxation enhancement for protein-observedRSC advances · 2016Article
- UTOPIA NMR: activating unexploited magnetization using interleaved low-gamma detection.Journal of biomolecular NMR · 2016Article
- Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes.Journal of biomolecular NMR · 2015Article
- ¹³Cα decoupling during direct observation of carbonyl resonances in solution NMR of isotopically enriched proteins.Journal of biomolecular NMR · 2014Article
- Acceleration of natural-abundance solid-state MAS NMR measurements on bone by paramagnetic relaxation from gadolinium-DTPA.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Customized metabolomics database for the analysis of NMR ¹H-¹H TOCSY and ¹³C-¹H HSQC-TOCSY spectra of complex mixtures.Analytical chemistry · 2014Article
- NMR structure analysis of uniformly 13C-labeled carbohydrates.Journal of biomolecular NMR · 2014Article
- Practical aspects of NMR signal assignment in larger and challenging proteins.Progress in nuclear magnetic resonance spectroscopy · 2014Review
- Improved NMR experiments with ¹³C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.Journal of biomolecular NMR · 2014Article
- Multidimensional approaches to NMR-based metabolomics.Analytical chemistry · 2014Review
- Protein folding on the ribosome studied using NMR spectroscopy.Progress in nuclear magnetic resonance spectroscopy · 2013Review
- Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes.Chemphyschem : a European journal of chemical physics and physical chemistry · 2013Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The assignment of the aliphatic (13)C resonances of trimeric Bacillus Subtilis chorismate mutase, a protein with a molecular mass of 44 kDa, consisting of three 127-residue monomers is presented by use of two-dimensional (2D) (13)C-start and (13)C-observe NMR experiments. These experiments start with (13)C excitation and end with (13)C observation while relying on the long transverse relaxation times of (13)C spins in uniformly deuterated and (13)C,(15)N-labeled large proteins. Gains in sensitivity are achieved by the use of a paramagnetic relaxation enhancement agent to reduce (13)C T(1) relaxation times with little effect on (13)C T(2) relaxation times. Such 2D (13)C-only NMR experiments circumvent problems associated with the application of conventional experiments for side-chain assignment to proteins of larger sizes, for instance, the absence or low concentration of the side-chain (1)H spins, the transfer of the side-chain spin polarization to the (1)H(N) spins for signal acquisition, or the necessity of a quantitative reprotonation of the methyl moieties in the otherwise fully deuterated side-chains. We demonstrate that having obtained a nearly complete assignment of the side-chain aliphatic (13)C resonances, the side-chain (1)H chemical shifts can be assigned in a semiautomatic fashion using 3D (15)N-resolved and (13)C-resolved NOESY experiments measured with a randomly partially protonated protein sample. We also discuss perspectives for structure determination of larger proteins by using novel strategies which are based on the (1)H,(1)H NOEs in combination with multiple residual dipolar couplings between adjacent (13)C spins determined with 2D (13)C-only experiments.
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