Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 32, Issue -, Pages 113-122Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2015.03.009
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Funding
- FRISBI within the Grenoble Partnership for Structural Biology (PSB) [ANR-10-INSB-05-02]
- GRAL within the Grenoble Partnership for Structural Biology (PSB) [ANR-10-LABX-49-01]
- European Research Council under the European Community [260887]
- European Research Council (ERC) [260887] Funding Source: European Research Council (ERC)
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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 NMR spectroscopy in the study of supra-molecular complexes with molecular weights of up to 1 MDa. At the core of these isotopic labeling developments is the specific introduction of [H-1,C-13]-labeled methyl probes into perdeuterated proteins. Here, we describe the evolution of these approaches and discuss their impact on structural and biological studies. The relevant protocols are succinctly reviewed for single and combinatorial isotopic-labeling of methyl-containing residues, and examples of applications on challenging biological systems, including high molecular weight and membrane proteins, are presented.
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