Backbone Assignment of Fully Protonated Solid Proteins by 1H Detection and Ultrafast Magic-Angle-Spinning NMR Spectroscopy

被引:85
作者
Marchetti, Alessandro [1 ,2 ]
Jehle, Stefan [1 ]
Felletti, Michele [1 ]
Knight, Michael J. [1 ]
Wang, Yao [3 ]
Xu, Zhi-Qiang [3 ]
Park, Ah Young [4 ]
Otting, Gottfried [4 ]
Lesage, Anne [1 ]
Emsley, Lyndon [1 ]
Dixon, Nicholas E. [3 ]
Pintacuda, Guido [1 ]
机构
[1] Univ Lyon, Ecole Normale Super Lyon, UMR CNRS 5280, Ctr RMN Tres Hauts Champs, F-69100 Villeurbanne, France
[2] Scuola Normale Super Pisa, I-56126 Pisa, Italy
[3] Univ Wollongong, Sch Chem, Wollongong, NSW 2522, Australia
[4] Australian Natl Univ, Res Sch Chem, Canberra, ACT 0200, Australia
基金
澳大利亚研究理事会;
关键词
DNA polymerase; magic-angle spinning; NMR spectroscopy; protein structures; scalar transfers; STATE NMR; STRUCTURAL BASIS; TERMINAL DOMAIN; MAS; RESOLUTION; PEPTIDES;
D O I
10.1002/anie.201203124
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Narrow 1H NMR linewidths can be obtained for fully protonated protein samples in the solid state by using ultrafast magic-angle spinning (60 kHz). Medium-size microcrystalline and noncrystalline proteins can be analyzed without any need for deuteration of the protein sample. This approach provides assignments of the backbone 1H, 15N, 13C α, and 13CO resonances and yields information about 1H-1H proximities. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码:10756 / 10759
页数:4
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