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- URN to cite this document:
- urn:nbn:de:bvb:355-epub-530379
- DOI to cite this document:
- 10.5283/epub.53037
Abstract
Nuclear magnetic resonance (NMR) methods that quantitatively probe motions on molecular and atomic levels have propelled the understanding of biomolecular processes for which static structures cannot provide a satisfactory description. In this work, we studied the structure and dynamics of the essential 100-kDa eukaryotic 5′→3′ exoribonuclease Xrn2. A combination of complementary fluorine and ...

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