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

被引：24

作者：

Smith, Albert A. ^{[1
]}

Ravotti, Francesco ^{[1
]}

Testori, Emilie ^{[1
]}

Cadalbert, Riccardo ^{[1
]}

Ernst, Matthias ^{[1
]}

Bockmann, Anja ^{[2
]}

Meier, Beat H. ^{[1
]}

机构：

[1] Swiss Fed Inst Technol, Phys Chem, Vladimir Prelog Weg 2, CH-8093 Zurich, Switzerland

[2] Univ Lyon, Inst Biol & Chim Prot, UMR CNRS 5086, Labex Ecofect,Bases Mol & Struct Syst Infectieux, 7 Passage Vercors, F-69367 Lyon, France

来源：

JOURNAL OF BIOMOLECULAR NMR | 2017年 / 67卷 / 02期

基金：

瑞士国家科学基金会;

关键词：

Solid-state NMR; Fibrils; Chemical shift assignment; Deuterium isotope effect; Deuterated proteins; Proton detection; STATE NMR-SPECTROSCOPY; S PRION PROTEIN; CHEMICAL-SHIFTS; RESONANCE ASSIGNMENT; HET-S; HETEROKARYON INCOMPATIBILITY; AMYLOID FIBRILS; 100; KHZ; C-13; RESOLUTION;

D O I：

10.1007/s10858-016-0087-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Fast magic-angle spinning and partial sample deuteration allows direct detection of H-1 in solid-state NMR, yielding significant gains in mass sensitivity. In order to further analyze the spectra, H-1 detection requires assignment of the H-1 resonances. In this work, resonance assignments of backbone H-N and H alpha are presented for HET-s(218-289) fibrils, based on the existing assignment of C alpha, C beta, C', and N resonances. The samples used are partially deuterated for higher spectral resolution, and the shifts in resonance frequencies of C alpha and C beta 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.

引用

页码：109 / 119

页数：11

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