Erratum to: 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
Erratum to: 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
Erratum to: 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
Content Type Journal Article
Category Erratum
Pages 1-1
DOI 10.1007/s10858-011-9562-9
Authors
Xun-Cheng Su, Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia
Choy-Theng Loh, Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia
Ruhu Qi, Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia
Gottfried Otting, Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia
Erratum to: Paramagnetic labelling of proteins and oligonucleotides for NMR
Erratum to: Paramagnetic labelling of proteins and oligonucleotides for NMR
Erratum to: Paramagnetic labelling of proteins and oligonucleotides for NMR
Content Type Journal Article
Pages 1-2
DOI 10.1007/s10858-011-9475-7
Authors
nmrlearner
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02-23-2011 11:21 PM
Erratum to: Paramagnetic labelling of proteins and oligonucleotides for NMR
Erratum to: Paramagnetic labelling of proteins and oligonucleotides for NMR
Erratum to: Paramagnetic labelling of proteins and oligonucleotides for NMR
Content Type Journal Article
Pages 1-2
DOI 10.1007/s10858-011-9475-7
Authors
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
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
Abstract Selectively isotope labelled protein samples can be prepared in vivo or in vitro from selectively labelled amino acids but, in many cases, metabolic conversions between different amino acids result in isotope scrambling. The best results are obtained by cell-free protein synthesis, where metabolic enzymes are generally less active, but isotope scrambling can never be suppressed completely. We show that...
nmrlearner
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02-16-2011 09:34 PM
Cell-free expression and stable isotope labelling strategies for membrane proteins
Cell-free expression and stable isotope labelling strategies for membrane proteins
Abstract Membrane proteins are highly underrepresented in the structural data-base and remain one of the most challenging targets for functional and structural elucidation. Their roles in transport and cellular communication, furthermore, often make over-expression toxic to their host, and their hydrophobicity and structural complexity make isolation and reconstitution a complicated task, especially in cases where proteins are targeted to inclusion bodies. The development of cell-free expression systems...
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01-09-2011 12:46 PM
[NMR paper] Cell-free synthesis of 15N-labeled proteins for NMR studies.
Cell-free synthesis of 15N-labeled proteins for NMR studies.
Related Articles Cell-free synthesis of 15N-labeled proteins for NMR studies.
IUBMB Life. 2005 Sep;57(9):615-22
Authors: Ozawa K, Dixon NE, Otting G
Modern cell-free in vitro protein synthesis systems present powerful tools for the synthesis of isotope-labeled proteins in high yields. The production of selectively 15 N-labeled proteins from 15 N-labeled amino acids is particularly economic and yields are often sufficient to analyze the proteins very quickly by two-dimensional NMR...
nmrlearner
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12-01-2010 06:56 PM
[NMR paper] Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for
Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis.
Related Articles Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis.
J Biomol NMR. 1995 Sep;6(2):129-34
Authors: Kigawa T, Muto Y, Yokoyama S
For the application of multidimensional NMR spectroscopy to larger proteins, it would be useful to perform selective labeling of one of the 20 amino acids. For some amino acids, however, amino acid metabolism drastically reduces the efficiency and selectivity...
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08-22-2010 03:50 AM
Cell-free protein synthesis of perdeuterated proteins for NMR studies
Cell-free protein synthesis of perdeuterated proteins for NMR studies
Touraj Etezady-Esfarjani, Sebastian Hiller, Cristina Villalba and Kurt Wüthrich
Journal of Biomolecular NMR; 2007; 39(3); pp 229-238
Abstract:
Cell-free protein synthesis protocols for uniformly deuterated proteins typically yield low, non-uniform deuteration levels. This paper introduces an E. coli cell-extract, D-S30, which enables efficient production of proteins with high deuteration levels for all non-labile hydrogen atom positions. Potential applications of the new protocol may include production of proteins...