Abstract
Complete 13C and 15N assignments of the B3 IgG-binding domain of protein G (GB3) in the microcrystalline solid phase, obtained using 2D and 3D MAS NMR, are presented. The chemical shifts are used to predict the protein backbone conformation and compared with solution-state shifts.
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Acknowledgments
This research was supported by the Ohio State University. The authors thank Dr. Ad Bax (National Institutes of Health) for the gift of the GB3 plasmid and Prof. Chad M. Rienstra (University of Illinois, Urbana-Champaign) for a control sample of 13C,15N-labeled GB1, sharing unpublished data for GB3 crystallized using the batch method, and stimulating discussions related to sample preparation, and experimental protocols.
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Nadaud, P.S., Helmus, J.J. & Jaroniec, C.P. 13C and 15N chemical shift assignments and secondary structure of the B3 immunoglobulin-binding domain of streptococcal protein G by magic-angle spinning solid-state NMR spectroscopy. Biomol NMR Assign 1, 117–120 (2007). https://doi.org/10.1007/s12104-007-9041-0
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DOI: https://doi.org/10.1007/s12104-007-9041-0