ArticleJournal of biomolecular NMR2006
Amino-acid type identification in 15N-HSQC spectra by combinatorial selective 15N-labelling.
Article in Journal of biomolecular NMR, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed.
- Amino-acid selective isotope labeling enables simultaneous overlapping signal decomposition and information extraction from NMR spectra.Journal of biomolecular NMR · 2020Article
- CombLabel: rational design of optimized sequence-specific combinatorial labeling schemes. Application to backbone assignment of membrane proteins with low stability.Journal of biomolecular NMR · 2019Article
- Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression.Biochemistry · 2016Article
- Stable isotope labeling strategy based on coding theory.Journal of biomolecular NMR · 2015Article
- An extended combinatorial 15N, 13Cα, and 13C' labeling approach to protein backbone resonance assignment.Journal of biomolecular NMR · 2015Article
- Time-shared experiments for efficient assignment of triple-selectively labeled proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Selective methyl labeling of eukaryotic membrane proteins using cell-free expression.Journal of the American Chemical Society · 2014Article
- Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, epsilon, θ and β reveals a highly flexible arrangement of the proofreading domain.Nucleic acids research · 2013Article
- Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment.Journal of biomolecular NMR · 2012Article
- Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins.Advances in experimental medicine and biology · 2012Review
- Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2011Article
- Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O.Journal of biomolecular NMR · 2011Article
- An economical method for producing stable-isotope labeled proteins by the E. coli cell-free system.Journal of biomolecular NMR · 2010Article
- Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Cell-free expression and stable isotope labelling strategies for membrane proteins.Journal of biomolecular NMR · 2010Article
- Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- Glutarate and N-acetyl-L-glutamate buffers for cell-free synthesis of selectively 15N-labelled proteins.Journal of biomolecular NMR · 2009Article
- Memory T cell RNA rearrangement programmed by heterogeneous nuclear ribonucleoprotein hnRNPLL.Immunity · 2008Article
- Prospects for lanthanides in structural biology by NMR.Journal of biomolecular NMR · 2008Article
- A systematic analysis of backbone amide assignments achieved via combinatorial selective labelling of amino acids.Journal of biomolecular NMR · 2007Article
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6 authors.
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Abstract
The efficiency of cell-free protein synthesis combined with combinatorial selective 15N-labelling provides a method for the rapid assignment of 15N-HSQC cross-peaks to the 19 different non-proline amino-acid types from five 15N-HSQC spectra. This strategy was explored with two different constructs of the C-terminal domain V of the tau subunit of the Escherichia coli DNA polymerase III holoenzyme, tauC16 and tauC14. Since each of the five 15N-HSQC spectra contained only about one third of the cross-peaks present in uniformly labelled samples, spectral overlap was much reduced. All 15N-HSQC cross-peaks of the backbone amides could be assigned to the correct amino-acid type. Availability of the residue-type information greatly assisted the evaluation of the changes in chemical shifts observed for corresponding residues in tauC16 vs. those in tauC14, and the analysis of the structure and mobility of the C-terminal residues present in tauC16 but not in tauC14.
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