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] (13)CHD 2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.
(13)CHD 2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.
Related Articles (13)CHD 2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.
J Biomol NMR. 2015 Aug 14;
Authors: Rennella E, Huang R, Velyvis A, Kay LE
Abstract
An NMR experiment for quantifying slow (millisecond) time-scale exchange processes involving the interconversion between visible ground state and invisible, conformationally excited...
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08-15-2015 04:01 PM
13 CHD 2 â??CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins
13 CHD 2 â??CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins
Abstract
An NMR experiment for quantifying slow (millisecond) time-scale exchange processes involving the interconversion between visible ground state and invisible, conformationally excited state conformers is presented. The approach exploits chemical exchange saturation transfer (CEST) and makes use of 13CHD2 methyl group probes that can be readily incorporated into otherwise highly deuterated proteins. The methodology is...
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08-14-2015 10:12 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
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] Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin r
Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme.
Related Articles Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme.
J Am Chem Soc. 2005 Jun 8;127(22):8214-25
Authors: Tugarinov V, Ollerenshaw JE, Kay LE
New NMR experiments for the measurement of side-chain dynamics in high molecular weight ( approximately 100 kDa) proteins are presented. The experiments quantify (2)H spin...
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11-25-2010 08:21 PM
[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...
NMRMethod for Characterizing Microsecond-to-MillisecondChemical Exchanges Utilizing Differential Multiple-Quantum Relaxationin High Molecular Weight Proteins
Linear Mode
