Application Note: Efficient Uniform Labeling of Proteins Expressed in Baculovirus-Infected Insect Cells Using ... - SelectScience
Application Note: Efficient Uniform Labeling of Proteins Expressed in Baculovirus-Infected Insect Cells Using ... - SelectScience
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Application Note: Efficient Uniform Labeling of Proteins Expressed in Baculovirus-Infected Insect Cells Using ...
SelectScience
Uniform isotope labeling is a key tool for NMR studies on recombinant proteins and their interaction with ligands of pharmaceutical interest. To be useful for most important NMR studies, a labeled protein has to be expressed with baculovirus-infected ...
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07-23-2017 11:38 AM
[NMR paper] CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample.
CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample.
Related Articles CH3-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample.
J Biomol NMR. 2015 Nov 13;
Authors: Kerfah R, Hamelin O, Boisbouvier J, Marion D
Abstract
A new strategy for the NMR assignment of aliphatic side-chains in large perdeuterated proteins is proposed. It involves an alternative isotopic...
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11-15-2015 07:55 PM
CH 3 -specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample
CH 3 -specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample
Abstract
A new strategy for the NMR assignment of aliphatic side-chains in large perdeuterated proteins is proposed. It involves an alternative isotopic labeling protocol, the use of an out-and-back 13Câ??13C TOCSY experiment ((H)C-TOCSY-C-TOCSY-(C)H) and an optimized non-uniform sampling protocol. It has long been known that the non-linearity of an aliphatic spin-system (for example Ile, Val, or Leu)...
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11-14-2015 03:37 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
Selective editing of Val and Leu methyl groups in high molecular weight protein NMR
Selective editing of Val and Leu methyl groups in high molecular weight protein NMR
Abstract The development of methyl-TROSY approaches and specific 13Câ??1H labeling of Ile, Leu and Val methyl groups in highly deuterated proteins has made it possible to study high molecular weight proteins, either alone or in complexes, using solution nuclear magnetic resonance (NMR) spectroscopy. Here we present 2-dimensional (2D) and 3-dimensional (3D) NMR experiments designed to achieve complete separation of the methyl resonances of Val and Leu, labeled using the same precursor, α-ketoisovalerate...
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05-01-2012 07:06 AM
An optimized isotopic labelling strategy of isoleucine-?(2) methyl groups for solution NMR studies of high molecular weight proteins.
An optimized isotopic labelling strategy of isoleucine-?(2) methyl groups for solution NMR studies of high molecular weight proteins.
An optimized isotopic labelling strategy of isoleucine-?(2) methyl groups for solution NMR studies of high molecular weight proteins.
Chem Commun (Camb). 2011 Jul 26;
Authors: Ayala I, Hamelin O, Amero C, Pessey O, Plevin MJ, Gans P, Boisbouvier J
An efficient synthetic route is proposed to produce 2-hydroxy-2-ethyl-3-oxobutanoate for the specific labelling of Ile methyl-?(2) groups in proteins. The (2)H,...
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07-28-2011 10:51 AM
Alanine Methyl Groups as NMR Probes of Molecular Structure and Dynamics in High-Molecular-Weight Proteins
Alanine Methyl Groups as NMR Probes of Molecular Structure and Dynamics in High-Molecular-Weight Proteins
Raquel Godoy-Ruiz, Chenyun Guo and Vitali Tugarinov
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1083656/aop/images/medium/ja-2010-083656_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1083656
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/hxZ4cabF688
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12-08-2010 10:04 AM
[NMR paper] Quantitative NMR studies of high molecular weight proteins: application to domain ori
Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G.
Related Articles Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G.
J Mol Biol. 2003 Apr 11;327(5):1121-33
Authors: Tugarinov V, Kay LE
A high-resolution multidimensional NMR study of ligand-binding to Escherichia coli malate synthase G (MSG), a 723-residue monomeric enzyme (81.4...
Application Note: Isotope Labeling of Alanine Methyl Groups for NMR Studies of High-Molecular-Weight Proteins - SelectScience
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