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Literature DB >> 20157899

Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins.

Pierre Gans¹, Olivier Hamelin, Remy Sounier, Isabel Ayala, M Asunción Durá, Carlos D Amero, Marjolaine Noirclerc-Savoye, Bruno Franzetti, Michael J Plevin, Jérôme Boisbouvier.

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Year: 2010 PMID： 20157899 DOI： 10.1002/anie.200905660

Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN： 1433-7851 Impact factor: 15.336

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80 in total

1. Estimating side-chain order in methyl-protonated, perdeuterated proteins via multiple-quantum relaxation violated coherence transfer NMR spectroscopy.

Authors: Hechao Sun; Raquel Godoy-Ruiz; Vitali Tugarinov
Journal: J Biomol NMR Date: 2012-03 Impact factor: 2.835

2. Thermal coefficients of the methyl groups within ubiquitin.

Authors: T Michael Sabo; Davood Bakhtiari; Korvin F A Walter; Robert L McFeeters; Karin Giller; Stefan Becker; Christian Griesinger; Donghan Lee
Journal: Protein Sci Date: 2012-03-02 Impact factor: 6.725

3. Optimal methyl labeling for studies of supra-molecular systems.

Authors: Tomasz L Religa; Lewis E Kay
Journal: J Biomol NMR Date: 2010-04-27 Impact factor: 2.835

4. Direct detection of CH/pi interactions in proteins.

Authors: Michael J Plevin; David L Bryce; Jérôme Boisbouvier
Journal: Nat Chem Date: 2010-05-02 Impact factor: 24.427

5. (13)CHD2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.

Authors: Enrico Rennella; Rui Huang; Algirdas Velyvis; Lewis E Kay
Journal: J Biomol NMR Date: 2015-08-14 Impact factor: 2.835

Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins.

1. Estimating side-chain order in methyl-protonated, perdeuterated proteins via multiple-quantum relaxation violated coherence transfer NMR spectroscopy.

2. Thermal coefficients of the methyl groups within ubiquitin.

3. Optimal methyl labeling for studies of supra-molecular systems.

4. Direct detection of CH/pi interactions in proteins.

5. (13)CHD2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.

6. A simple biosynthetic method for stereospecific resonance assignment of prochiral methyl groups in proteins.

7. Selective editing of Val and Leu methyl groups in high molecular weight protein NMR.

8. Independent valine and leucine isotope labeling in Escherichia coli protein overexpression systems.

9. Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.

10. Mutation of Conserved Mre11 Residues Alter Protein Dynamics to Separate Nuclease Functions.