Literature DB >> 28074361

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

Albert A Smith1, Francesco Ravotti1, Emilie Testori1, Riccardo Cadalbert1, Matthias Ernst2, Anja Böckmann3, Beat H Meier4.   

Abstract

Fast magic-angle spinning and partial sample deuteration allows direct detection of 1H in solid-state NMR, yielding significant gains in mass sensitivity. In order to further analyze the spectra, 1H detection requires assignment of the 1H resonances. In this work, resonance assignments of backbone HN 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.

Entities:  

Keywords:  Chemical shift assignment; Deuterated proteins; Deuterium isotope effect; Fibrils; Proton detection; Solid-state NMR

Mesh：

Substances：

Year:  2017        PMID： 28074361     DOI： 10.1007/s10858-016-0087-0

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN： 0925-2738            Impact factor:   2.835


  31 in total

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