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Isotope labeling methods for large systems.

Authors
  • Lundström, Patrik
  • Ahlner, Alexandra
  • Blissing, Annica Theresia
Type
Published Article
Journal
Advances in experimental medicine and biology
Publication Date
Jan 01, 2012
Volume
992
Pages
3–15
Identifiers
DOI: 10.1007/978-94-007-4954-2_1
PMID: 23076576
Source
Medline
License
Unknown

Abstract

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.

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