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

被引：0
作者：
Albert A. Smith
Francesco Ravotti
Emilie Testori
Riccardo Cadalbert
Matthias Ernst
Anja Böckmann
Beat H. Meier
机构：
[1] ETH Zürich,
[2] Physical Chemistry,undefined
[3] Institut de Biologie et Chimie des Protéines,undefined
[4] Bases Moléculaires et Structurales des Systèmes Infectieux,undefined
[5] Labex Ecofect,undefined
[6] UMR 5086 CNRS,undefined
[7] Université de Lyon,undefined
来源：
Journal of Biomolecular NMR | 2017年 / 67卷
关键词：
Solid-state NMR; Fibrils; Chemical shift assignment; Deuterium isotope effect; Deuterated proteins; Proton detection;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
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.
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页码：109 / 119
页数：10
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