NMR studies of large protein systems

Shiou Ru Tzeng, Ming Tao Pai, Charalampos G. Kalodimos

Research output: Chapter in Book/Report/Conference proceedingChapter

30 Scopus citations

Abstract

Over the recent years, there has been increased interest in applying NMR spectroscopy for the characterization of proteins and protein complexes of large molecular weight. The combination of multidimensional NMR, novel pulse sequences allowing for the selection of slowly relaxing coherence pathways, and the development of a range of labeling techniques has enabled high-resolution NMR analyses of supramolecular systems of even megadalton size. Here, we describe how NMR can be used to obtain structural information in large systems by using as an example the recent structure determination of SecA ATPase (204 kDa) in complex with a signal peptide.

Original languageEnglish (US)
Title of host publicationProtein NMR Techniques
Pages133-140
Number of pages8
DOIs
StatePublished - 2012

Publication series

NameMethods in Molecular Biology
Volume831
ISSN (Print)1064-3745

Keywords

  • Macromolecular complex
  • Molecular machinery
  • Paramagnetic resonance enhancement
  • Stable isotope labeling

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