| Literature DB >> 26280528 |
Thomas Wiegand1, Carole Gardiennet2, Francesco Ravotti1, Alexandre Bazin2, Britta Kunert2, Denis Lacabanne2, Riccardo Cadalbert1, Peter Güntert1,3, Laurent Terradot4, Anja Böckmann5, Beat H Meier6.
Abstract
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.Entities:
Keywords: Assignments; HpDnaB; Secondary chemical shifts; Solid-state NMR; ssFLYA
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Year: 2015 PMID: 26280528 DOI: 10.1007/s12104-015-9629-8
Source DB: PubMed Journal: Biomol NMR Assign ISSN: 1874-270X Impact factor: 0.746