ArticleJournal of biomolecular NMR2016
Sparse (13)C labelling for solid-state NMR studies of P. pastoris expressed eukaryotic seven-transmembrane proteins.
Article in Journal of biomolecular NMR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Production of isotope-labeled nanobody KN035 inMagnetic resonance letters · 2026Article
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- Super-Resolution solid-state NMR Spectroscopy.Journal of biomolecular NMR · 2026Article
- Expression ofEPJ web of conferences · 2023Article
- Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR.Chemical science · 2021Review
- Improved Protocol for the Production of the Low-Expression Eukaryotic Membrane Protein Human Aquaporin 2 inBiomolecules · 2020Article
- Codon Harmonization of a Kir3.1-KirBac1.3 Chimera for Structural Study Optimization.Biomolecules · 2020Article
- Enhancing sensitivity of Double Electron-Electron Resonance (DEER) by using Relaxation-Optimized Acquisition Length Distribution (RELOAD) scheme.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Article
- Methyl-selective isotope labeling using α-ketoisovalerate for the yeast Pichia pastoris recombinant protein expression system.Journal of biomolecular NMR · 2018Article
- On the use of Pichia pastoris for isotopic labeling of human GPCRs for NMR studies.Journal of biomolecular NMR · 2018Review
- GdJournal of biomolecular NMR · 2017Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We demonstrate a novel sparse (13)C labelling approach for methylotrophic yeast P. pastoris expression system, towards solid-state NMR studies of eukaryotic membrane proteins. The labelling scheme was achieved by co-utilizing natural abundance methanol and specifically (13)C labelled glycerol as carbon sources in the expression medium. This strategy improves the spectral resolution by 1.5 fold, displays site-specific labelling patterns, and has advantages for collecting long-range distance restraints for structure determination of large eukaryotic membrane proteins by solid-state NMR.
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