ArticleJournal of biomolecular NMR2018
Methyl-selective isotope labeling using α-ketoisovalerate for the yeast Pichia pastoris recombinant protein expression system.
Article in Journal of biomolecular NMR, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Production of isotope-labeled nanobody KN035 inMagnetic resonance letters · 2026Article
- A random fractionalMagnetic resonance letters · 2026Article
- Methyl-specific NMR of therapeutic antibodies: cost-effective isotopic labeling strategies in CHO cells for high-resolution structural characterization.Journal of biomolecular NMR · 2026Article
- Construction and Identification of a Breast Bioreactor for Human-Derived Hypoglycemic Protein Amylin.Life (Basel, Switzerland) · 2024Article
- α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.Annual review of physical chemistry · 2021Review
- High-resolution ex vivo NMR spectroscopy of human Z αNature communications · 2020Article
- Improved strategy for isoleucineJournal of biomolecular NMR · 2019Article
- Automatic structure-based NMR methyl resonance assignment in large proteins.Nature communications · 2019Article
- Emerging solution NMR methods to illuminate the structural and dynamic properties of proteins.Current opinion in structural biology · 2019Review
- Isotopic Labeling of Eukaryotic Membrane Proteins for NMR Studies of Interactions and Dynamics.Methods in enzymology · 2019Article
- On the use of Pichia pastoris for isotopic labeling of human GPCRs for NMR studies.Journal of biomolecular NMR · 2018Review
- Advanced isotopic labeling for the NMR investigation of challenging proteins and nucleic acids.Journal of biomolecular NMR · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Methyl-detected NMR spectroscopy is a useful tool for investigating the structures and interactions of large macromolecules such as membrane proteins. The procedures for preparation of methyl-specific isotopically-labeled proteins were established for the Escherichia coli (E. coli) expression system, but typically it is not feasible to express eukaryotic proteins using E. coli. The Pichia pastoris (P. pastoris) expression system is the most common yeast expression system, and is known to be superior to the E. coli system for the expression of mammalian proteins, including secretory and membrane proteins. However, this system has not yet been optimized for methyl-specific isotope labeling, especially for Val/Leu-methyl specific isotope incorporation. To overcome this difficulty, we explored various culture conditions for the yeast cells to efficiently uptake Val/Leu precursors. Among the searched conditions, we found that the cultivation pH has a critical effect on Val/Leu precursor uptake. At an acidic cultivation pH, the uptake of the Val/Leu precursor was increased, and methyl groups of Val and Leu in the synthesized recombinant protein yielded intense
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