Wiegand Thomas, Gardiennet Carole, Ravotti Francesco, Bazin Alexandre, Kunert Britta, Lacabanne Denis, Cadalbert Riccardo, Güntert Peter, Terradot Laurent, Böckmann Anja, Meier Beat H
Laboratorium für Physikalische Chemie, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland.
Institut de Biologie et Chemie des Protéines, Bases Moléculaires et Structurales des Systèmes Infectieux, Labex Ecofect, UMR 5086 CNRS, Université de Lyon, 7 passage du Vercor, 69007, Lyon, France.
Biomol NMR Assign. 2016 Apr;10(1):13-23. doi: 10.1007/s12104-015-9629-8. Epub 2015 Aug 18.
We present solid-state NMR assignments of the N-terminal domain of the DnaB helicase from Helicobacter pylori (153 residues) in its microcrystalline form. We use a sequential resonance assignment strategy based on three-dimensional NMR experiments. The resonance assignments obtained are compared with automated resonance assignments computed with the ssFLYA algorithm. An analysis of the (13)C secondary chemical shifts determines the position of the secondary structure elements in this α-helical protein.
我们展示了幽门螺杆菌DnaB解旋酶N端结构域（153个残基）微晶形式的固态核磁共振归属。我们使用基于三维核磁共振实验的序列共振归属策略。将获得的共振归属与用ssFLYA算法计算的自动共振归属进行比较。对（13）C二级化学位移的分析确定了这种α螺旋蛋白中二级结构元件的位置。
