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      Partially-deuterated samples of HET-s(218-289) fibrils: assignment and deuterium isotope effect.

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          Abstract

          Fast magic-angle spinning and partial sample deuteration allows direct detection of (1)H in solid-state NMR, yielding significant gains in mass sensitivity. In order to further analyze the spectra, (1)H detection requires assignment of the (1)H resonances. In this work, resonance assignments of backbone H(N) and Hα are presented for HET-s(218-289) fibrils, based on the existing assignment of Cα, Cβ, C', and N resonances. The samples used are partially deuterated for higher spectral resolution, and the shifts in resonance frequencies of Cα and Cβ due to the deuterium isotope effect are investigated. It is shown that the deuterium isotope effect can be estimated and used for assigning resonances of deuterated samples in solid-state NMR, based on known resonances of the protonated protein.

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          Author and article information

          Journal
          J. Biomol. NMR
          Journal of biomolecular NMR
          Springer Nature
          1573-5001
          0925-2738
          Jan 10 2017
          Affiliations
          [1 ] ETH Zürich, Physical Chemistry, Vladimir-Prelog-Weg 2, 8093, Zürich, Switzerland.
          [2 ] ETH Zürich, Physical Chemistry, Vladimir-Prelog-Weg 2, 8093, Zürich, Switzerland. maer@ethz.ch.
          [3 ] Institut de Biologie et Chimie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercors, 69367, Lyon, France. a.bockmann@ibcp.fr.
          [4 ] ETH Zürich, Physical Chemistry, Vladimir-Prelog-Weg 2, 8093, Zürich, Switzerland. beme@ethz.ch.
          Article
          10.1007/s10858-016-0087-0
          10.1007/s10858-016-0087-0
          28074361
          716c75ef-af8c-4a9f-9da5-535523203288
          History

          Chemical shift assignment,Deuterated proteins,Deuterium isotope effect,Fibrils,Proton detection,Solid-state NMR

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