ArticleJournal of biomolecular NMR2004
Uniform and residue-specific 15N-labeling of proteins on a highly deuterated background.
Article in Journal of biomolecular NMR, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 76 citations in OpenAlex.
- NMR in the Age of Modern Biomedical Research and Drug Discovery.Journal of molecular biology · 2025Review
- Efficient Segmental Isotope Labeling of Integral Membrane Proteins for High-Resolution NMR Studies.Journal of the American Chemical Society · 2024Article
- NMR characterization of RNA binding property of the DEAD-box RNA helicase DDX3X and its implications for helicase activity.Nature communications · 2024Article
- Molecular Basis of Ca(II)-Induced Tetramerization and Transition-Metal Sequestration in Human Calprotectin.Journal of the American Chemical Society · 2021Article
- Enabling NMR Studies of High Molecular Weight Systems Without the Need for Deuteration: The XL-ALSOFAST Experiment with Delayed Decoupling.Angewandte Chemie (International ed. in English) · 2020Article
- Alpha protons as NMR probes in deuterated proteins.Journal of biomolecular NMR · 2019Article
- Improving yields of deuterated, methyl labeled protein by growing in HJournal of biomolecular NMR · 2018Article
- Cost-effective large-scale expression of proteins for NMR studies.Journal of biomolecular NMR · 2018Article
- Enhanced biosynthetically directed fractional carbon-13 enrichment of proteins for backbone NMR assignments.Protein expression and purification · 2015Article
- Facing and Overcoming Sensitivity Challenges in Biomolecular NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2015Review
- Spectroscopic studies reveal that the heme regulatory motifs of heme oxygenase-2 are dynamically disordered and exhibit redox-dependent interaction with heme.Biochemistry · 2015Article
- Differential ubiquitin binding by the acidic loops of Ube2g1 and Ube2r1 enzymes distinguishes their Lys-48-ubiquitylation activities.The Journal of biological chemistry · 2015Article
- Structural features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy.The Journal of biological chemistry · 2015Article
- Using ¹⁵N-ammonium to characterise and map potassium binding sites in proteins by NMR spectroscopy.Chembiochem : a European journal of chemical biology · 2014Article
- Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.Advances in experimental medicine and biology · 2012Review
- Expression and purification of Src-family kinases for solution NMR studies.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.Protein science : a publication of the Protein Society · 2011Article
- Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: insight into intrinsically disordered proteins.The Journal of biological chemistry · 2011Article
- Isotope labeling strategies for NMR studies of RNA.Journal of biomolecular NMR · 2010Review
- A general and efficient approach for NMR studies of peptide dynamics in class I MHC peptide binding grooves.Biochemistry · 2009Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A general method for stable-isotope labeling of large proteins is introduced and applied for studies of the E. coli GroE chaperone proteins by solution NMR. In addition to enabling the residue-specific (15)N-labeling of proteins on a highly deuterated background, it is also an efficient approach for uniform labeling. The method meets the requirements of high-level deuteration, minimal cross-labeling and high protein yield, which are crucial for NMR studies of structures with sizes above 150 kDa. The results obtained with the new protocol are compared to other strategies for protein labeling, and evaluated with regard to the influence of external factors on the resulting isotope labeling patterns. Applications with the GroE system show that these strategies are efficient tools for studies of structure, dynamics and intermolecular interactions in large supramolecular complexes, when combined with TROSY- and CRINEPT-based experimental NMR schemes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.