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Protein NMR spectroscopy

Hydrogen bonds under pressure

Nature Chemistry volume 4, pages 693–695 (2012)Cite this article

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Hydrogen bonds play a key role in defining the folding of proteins and the maintenance of their structure. A high-pressure NMR study of ubiquitin now provides unprecedented detail on the temperature and pressure dependence of its hydrogen-bond network.

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Figure 1: Pressure and temperature perturbations of ubiquitin.

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Acknowledgements

The authors are supported by the EU-funded project Bio-NMR. H.S. is member of the Deutsche Forschungsgemeinschaft-funded cluster of excellence: macromolecular complexes.

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  1. Gerd Nielsen and Harald Schwalbe are in the Center for Biomolecular NMR Spectroscopy, Institute for Organic Chemistry and Chemical Biology, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438 Frankfurt/Main, Germany,

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  1. Gerd Nielsen
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  2. Harald Schwalbe
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Correspondence to Harald Schwalbe.

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Nielsen, G., Schwalbe, H. Hydrogen bonds under pressure. Nature Chem 4, 693–695 (2012). https://doi.org/10.1038/nchem.1443

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