Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
November 17, 2014
Very Important Paper: Unambiguous Assignment of Short- and Long-Range Structural Restraints by Solid-State NMR using Segmental Isotope Labeling
Tobias Schubeis, Torsten Lührs, Christiane Ritter*
Solid-state NMR has become a powerful technique for the elucidation of the structures of large protein complexes. However, spectral complexity and sensitivity remain serious challenges. Protein trans-splicing by the split intein DnaE from Nostoc punctiforme allows specific segments of a full-length protein to be isotopically labeled under a wide variety of conditions. Christiane Ritter (Helmholtz Centre for Infection Research, Germany) and co-workers have now employed this approach to obtain solid-state NMR spectra of a fungal prion protein (HET-s) with significantly improved spectral quality. Protein trans-splicing can be easily combined with other isotope labeling strategies to facilitate the resonance assignment and collection of structural restraints of proteins by solid-state NMR.
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