Related ArticlesMethyl-Specific Isotope Labeling Strategies for NMR Studies of Membrane Proteins.
Methods Mol Biol. 2017;1635:109-123
Authors: Kurauskas V, Schanda P, Sounier R
Abstract
Methyl groups are very useful probes of structure, dynamics, and interactions in protein NMR spectroscopy. In particular, methyl-directed experiments provide high sensitivity even in very large proteins, such as membrane proteins in a membrane-mimicking environment. In this chapter, we discuss the approach for labeling methyl groups in E. coli-based protein expression, as exemplified with the mitochondrial carrier GGC.
[NMR paper] Isotope-labeling strategies for solution NMR studies of macromolecular assemblies.
Isotope-labeling strategies for solution NMR studies of macromolecular assemblies.
Related Articles Isotope-labeling strategies for solution NMR studies of macromolecular assemblies.
Curr Opin Struct Biol. 2016 Jun 10;38:75-82
Authors: Zhang H, van Ingen H
Abstract
Proteins come together in macromolecular assemblies, recognizing and binding to each other through their structures, and operating on their substrates through their motions. Detailed characterization of these processes is particularly suited to NMR, a high-resolution...
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06-14-2016 08:23 PM
[NMR paper] Exploiting E. coli auxotrophs for leucine, valine, and threonine specific methyl labeling of large proteins for NMR applications.
Exploiting E. coli auxotrophs for leucine, valine, and threonine specific methyl labeling of large proteins for NMR applications.
Exploiting E. coli auxotrophs for leucine, valine, and threonine specific methyl labeling of large proteins for NMR applications.
J Biomol NMR. 2016 Jun 2;
Authors: Monneau YR, Ishida Y, Rossi P, Saio T, Tzeng SR, Inouye M, Kalodimos CG
Abstract
A simple and cost effective method to independently and stereo-specifically incorporate -methyls in Leu and Val in proteins is presented. Recombinant proteins...
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06-04-2016 11:08 AM
Exploiting E. coli auxotrophs for leucine, valine, and threonine specific methyl labeling of large proteins for NMR applications
Exploiting E. coli auxotrophs for leucine, valine, and threonine specific methyl labeling of large proteins for NMR applications
Abstract
A simple and cost effective method to independently and stereo-specifically incorporate -methyls in Leu and Val in proteins is presented. Recombinant proteins for NMR studies are produced using a tailored set of auxotrophic E. coli strains. NMR active isotopes are routed to either Leu or Val methyl groups from the commercially available and scrambling-free precursors α-ketoisovalerate and acetolactate. The...
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06-03-2016 04:52 PM
[NMR paper] Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins.
Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins.
Related Articles Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins.
Curr Opin Struct Biol. 2015 Apr 13;32:113-122
Authors: Kerfah R, Plevin MJ, Sounier R, Gans P, Boisbouvier J
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is a uniquely powerful tool for studying the structure, dynamics and interactions of biomolecules at atomic resolution. In the past 15 years, the...
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04-17-2015 08:49 PM
Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins
Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins
Publication date: June 2015
Source:Current Opinion in Structural Biology, Volume 32</br>
Author(s): Rime Kerfah , Michael J Plevin , Remy Sounier , Pierre Gans , Jerome Boisbouvier</br>
Nuclear magnetic resonance (NMR) spectroscopy is a uniquely powerful tool for studying the structure, dynamics and interactions of biomolecules at atomic resolution. In the past 15 years, the development of new isotopic labeling strategies has opened the possibility of exploiting...
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04-14-2015 01:24 PM
[NMR paper] Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins.
Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins.
J Biomol NMR. 2013 Sep 28;
Authors: Mas G, Crublet E, Hamelin O, Gans P, Boisbouvier J
Abstract
The specific protonation of valine and leucine methyl...
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10-01-2013 11:15 PM
Isotope labeling strategies for NMR studies of RNA
Isotope labeling strategies for NMR studies of RNA
Abstract The known biological functions of RNA have expanded in recent years and now include gene regulation, maintenance of sub-cellular structure, and catalysis, in addition to propagation of genetic information. As for proteins, RNA function is tightly correlated with structure. Unlike proteins, structural information for larger, biologically functional RNAs is relatively limited. NMR signal degeneracy, relaxation problems, and a paucity of long-range 1Hâ??1H dipolar contacts have limited the utility of traditional NMR approaches....
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01-09-2011 12:46 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...
Methyl-Specific Isotope Labeling Strategies for NMR Studies of Membrane Proteins.
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