ArticleJournal of biomolecular NMR2007
1-13C amino acid selective labeling in a 2H15N background for NMR studies of large proteins.
Article in Journal of biomolecular NMR, 2007. 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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30 citing papers in PubMed.
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- Specific isotopic labelling and reverse labelling for protein NMR spectroscopy: using metabolic precursors in sample preparation.Biochemical Society transactions · 2022Review
- Segmental and site-specific isotope labelling strategies for structural analysis of posttranslationally modified proteins.RSC chemical biology · 2021Review
- Mapping temperature-dependent conformational change in the voltage-sensing domain of an engineered heat-activated KProceedings of the National Academy of Sciences of the United States of America · 2021Article
- NMR Structural Analysis of Isolated Shaker Voltage-Sensing Domain in LPPG Micelles.Biophysical journal · 2019Article
- Probing Protein-Protein Interactions Using Asymmetric Labeling and Carbonyl-Carbon Selective Heteronuclear NMR Spectroscopy.Molecules (Basel, Switzerland) · 2018Review
- Selective labeling and unlabeling strategies in protein solid-state NMR spectroscopy.Journal of biomolecular NMR · 2018Review
- Role of protein dynamics in ion selectivity and allosteric coupling in the NaK channel.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Enhanced biosynthetically directed fractional carbon-13 enrichment of proteins for backbone NMR assignments.Protein expression and purification · 2015Article
- An extended combinatorial 15N, 13Cα, and 13C' labeling approach to protein backbone resonance assignment.Journal of biomolecular NMR · 2015Article
- NMR resonance assignments of the catalytic domain of human serine/threonine phosphatase calcineurin in unligated and PVIVIT-peptide-bound states.Biomolecular NMR assignments · 2015Article
- Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.Journal of biomolecular NMR · 2013Article
- Allosteric inhibition through suppression of transient conformational states.Nature chemical biology · 2013Article
- Structural and dynamic insights into substrate binding and catalysis of human lipocalin prostaglandin D synthase.Journal of lipid research · 2013Article
- Chemical shift prediction for denatured proteins.Journal of biomolecular NMR · 2013Article
- Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment.Journal of biomolecular NMR · 2012Article
- NMR and mutational identification of the collagen-binding site of the chaperone Hsp47.PloS one · 2012Article
- Assignment of backbone resonances in a eukaryotic protein kinase - ERK2 as a representative example.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Specific labeling of threonine methyl groups for NMR studies of protein-nucleic acid complexes.Biochemistry · 2011Article
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4 authors.
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Abstract
Isotope labeling by residue type (LBRT) has long been an important tool for resonance assignments at the limit where other approaches, such as triple-resonance experiments or NOESY methods do not succeed in yielding complete assignments. While LBRT has become less important for small proteins it can be the method of last resort for completing assignments of the most challenging protein systems. Here we present an approach where LBRT is achieved by adding protonated (14)N amino acids that are (13)C labeled at the carbonyl position to a medium for uniform deuteration and (15)N labeling. This has three important benefits over conventional (15)N LBRT in a deuterated back ground: (1) selective TROSY-HNCO cross peaks can be observed with high sensitivity for amino-acid pairs connected by the labeling, and the amide proton of the residue following the (13)C labeled amino acid is very sharp since its alpha position is deuterated, (2) the (13)C label at the carbonyl position is less prone to scrambling than the (15)N at the alpha-amino position, and (3) the peaks for the 1-(13)C labeled amino acids can be identified easily from the large intensity reduction in the (1)H-(15)N TROSY-HSQC spectrum for some residues that do not significantly scramble nitrogens, such as alanine and tyrosine. This approach is cost effective and has been successfully applied to proteins larger than 40 kDa.
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