[NMR paper] Cell-Free Protein Synthesis of Small Intrinsically Disordered Proteins for NMR Spectroscopy.
Cell-Free Protein Synthesis of Small Intrinsically Disordered Proteins for NMR Spectroscopy.
Related Articles Cell-Free Protein Synthesis of Small Intrinsically Disordered Proteins for NMR Spectroscopy.
Methods Mol Biol. 2020;2141:233-245
Authors: Isaksson L, Pedersen A
Abstract
Cell-free protein synthesis (CFPS) is an established method to produce recombinant proteins and has been used in a wide variety of applications. The use of CFPS has almost from the onset been favorably linked to the production of isotopically...
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07-23-2020 11:23 PM
[NMR paper] Protein labeling strategies for liquid-state NMR spectroscopy using cell-free synthesis.
Protein labeling strategies for liquid-state NMR spectroscopy using cell-free synthesis.
Related Articles Protein labeling strategies for liquid-state NMR spectroscopy using cell-free synthesis.
Prog Nucl Magn Reson Spectrosc. 2018 Apr;105:1-22
Authors: Hoffmann B, Löhr F, Laguerre A, Bernhard F, Dötsch V
Abstract
Preparation of a protein sample for liquid-state nuclear magnetic resonance (NMR) spectroscopy analysis requires optimization of many parameters. This review describes labeling strategies for obtaining assignments of...
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03-20-2018 10:11 PM
[NMR paper] Sequential Protein Expression and Capsid Assembly In Cell: Towards the Study of Multi-Protein Viral Capsids Using Solid-State NMR Techniques.
Sequential Protein Expression and Capsid Assembly In Cell: Towards the Study of Multi-Protein Viral Capsids Using Solid-State NMR Techniques.
Related Articles Sequential Protein Expression and Capsid Assembly In Cell: Towards the Study of Multi-Protein Viral Capsids Using Solid-State NMR Techniques.
Biochemistry. 2018 Feb 21;:
Authors: Alphonse S, Itin B, Khayat R, Ghose R
Abstract
While solid-state NMR (ssNMR) has emerged as a powerful technique to study viral capsids, current studies are limited to capsids formed from single...
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02-23-2018 03:44 AM
[NMR paper] Towards structural studies of self-assembled subviral particles: combining cell-free expression with 100 kHz MAS NMR.
Towards structural studies of self-assembled subviral particles: combining cell-free expression with 100 kHz MAS NMR.
Related Articles Towards structural studies of self-assembled subviral particles: combining cell-free expression with 100 kHz MAS NMR.
Angew Chem Int Ed Engl. 2018 Feb 19;:
Authors: David G, Fogeron ML, Schledorn M, Montserret R, Haselmann U, Penzel S, Badillo A, Lecoq L, André P, Nassal M, Bartenschlager R, Meier BH, Böckmann A
Abstract
Viral membrane proteins are prime targets in the combat against infection....
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02-21-2018 12:45 AM
Protein labeling strategies for liquid-state NMR spectroscopy using cell-free synthesis
Protein labeling strategies for liquid-state NMR spectroscopy using cell-free synthesis
Publication date: Available online 7 December 2017
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Beate Hoffmann, Frank Löhr, Aisha Laguerre, Frank Bernhard, Volker Dötsch</br>
Preparation of a protein sample for liquid-state nuclear magnetic resonance (NMR) spectroscopy analysis requires optimization of many parameters. This review describes labeling strategies for obtaining assignments of protein resonances. Particular emphasis is placed on...
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12-09-2017 07:49 AM
Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression
Combining in Vitro Folding with Cell Free Protein Synthesis for Membrane Protein Expression
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00488/20160721/images/medium/bi-2016-00488z_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00488
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/cYFGIK8-8JE
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07-22-2016 01:34 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...
Combining Cell-Free Protein Synthesis and NMR Into a Tool to Study Capsid Assembly Modulation - Frontiers
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