Watching protein structure at work in living cells using NMR spectroscopy
 

Watching protein structure at work in living cells using NMR spectroscopy

December 2012
Publication year: 2012
Source:Current Opinion in Chemical Biology, Volume 16, Issues 5–6</br>
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Isotope-assisted multi-dimensional NMR spectroscopy can now be applied to proteins inside living cells. The technique, called in-cell NMR, aims to investigate the structures, interactions and dynamics of proteins under their native conditions, ideally at an atomic resolution. The application has begun with bacterial cells but has now expanded to mammalian cultured cells, such as HeLa cells. The importance of the realization of such ‘in-mammalian cell’ NMR should be stressed, as these are the cells most often employed in cell biology. Hence, a substantially wide range of application would be possible in the near future once the technique has been well developed.
Highlights

? Advances in in-cell NMR spectroscopy of biomacromolecules. ? Escherichia coli, yeasts, Xenopus laevis oocytes and mammalian cell lines can be used. ? Structures, dynamics and interactions of proteins in living cells are studied. ? Proteins in the intracellular space behave differently from those in vitro.</br>
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