Isotope Labeling Methods for Large Systems

  • Patrik LundströmEmail author
  • Alexandra Ahlner
  • Annica Theresia Blissing
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 992)


A major drawback of nuclear magnetic resonance (NMR) spectroscopy compared to other methods is that the technique has been limited to relatively small molecules. However, in the last two decades the size limit has been pushed upwards considerably and it is now possible to use NMR spectroscopy for structure calculations of proteins of molecular weights approaching 100 kDa and to probe dynamics for supramolecular complexes of molecular weights in excess of 500 kDa. Instrumental for this progress has been development in instrumentation and pulse sequence design but also improved isotopic labeling schemes that lead to increased sensitivity as well as improved spectral resolution and simplification. These are described and discussed in this chapter, focusing on labeling schemes for amide proton and methyl proton detected experiments. We also discuss labeling methods for other potentially useful positions in proteins.


Nuclear Magnetic Resonance Nuclear Magnetic Resonance Spectroscopy Amide Proton Nuclear Overhauser Effect Residual Dipolar Coupling 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media Dordrecht 2012

Authors and Affiliations

  • Patrik Lundström
    • 1
    Email author
  • Alexandra Ahlner
    • 1
  • Annica Theresia Blissing
    • 1
  1. 1.Division of Molecular Biotechnology, Department of Physics, Chemistry and BiologyLinköping UniversityLinköpingSweden

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