Stereospecific Isotopic Labeling of Methyl Groups for NMR Spectroscopic Studies of High-Molecular-Weight Proteins

Pierre Gans (1) , Olivier Hamelin (2) , Rémy Sounier (1, 3) , Isabel Ayala (1) , M Asunción Durá (1) , Carlos D Amero (1) , Marjolaine Noirclerc-Savoye (1) , Bruno Franzetti (1) , Michael J Plevin (1) , Jérôme Boisbouvier (1)

1 IBS - UMR 5075 - Institut de biologie structurale
2 LCBM - UMR 5249 - Laboratoire de Chimie et Biologie des Métaux
3 HMS - Harvard Medical School [Boston]

Sometimes less is more: [13C1H3]methyl isotopomers can be biosynthetically incorporated specifically into the pro-S methyl groups of leucine and valine residues in large protein assemblies within a perdeuterated background by using an acetolactate precursor. This stereospecific labeling strategy considerably enhances NMR spectra for large protein assemblies.

Mots clés: NMR spectroscopy; isotopic labeling; MALATE-SYNTHASE-G; methyl-group labeling; DYNAMICS; RESIDUES; PRECURSOR; VALINE; N-15; ASSIGNMENTS; C-13; SUPRAMOLECULAR COMPLEXES; stereospecific protonation; STRATEGY; protein assemblies

Domaines: Biologie structurale [q-bio.BM]; Biophysique

Pierre Gans, Olivier Hamelin, Rémy Sounier, Isabel Ayala, M Asunción Durá, et al.. Stereospecific Isotopic Labeling of Methyl Groups for NMR Spectroscopic Studies of High-Molecular-Weight Proteins. Angewandte Chemie International Edition, 2010, 49 (11), pp.1958-1962. ⟨10.1002/anie.200905660⟩. ⟨hal-01143348⟩