Abstract
A first step toward the analysis of the structure, dynamics, and interactions of proteins by NMR is obtaining an acceptable level of resonance assignments. This process is nontrivial in most eukaryotic kinases given their size and suboptimal behavior in solution. Using inactive ERK2 as a representative example, we describe the procedures we utilized to achieve a significant degree of completeness of backbone resonance assignment.
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Acknowledgments
This research has been supported by the following grants from the National Institutes of Health: GM084278 (to RG), GM059802 (to KND), and 5G12 RR03060 (toward partial support of the NMR facilities at The City College of New York). RG is a member of the New York Structural Biology Center, NYSTAR facility. KND is a recipient of a grant from the Welch Foundation (F-1390). The authors thank Dr. Pia Vogel (SMU) for the kind gift of spin-labeled ATP.
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Piserchio, A., Dalby, K.N., Ghose, R. (2012). Assignment of Backbone Resonances in a Eukaryotic Protein Kinase – ERK2 as a Representative Example. In: Shekhtman, A., Burz, D. (eds) Protein NMR Techniques. Methods in Molecular Biology, vol 831. Humana Press. https://doi.org/10.1007/978-1-61779-480-3_19
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DOI: https://doi.org/10.1007/978-1-61779-480-3_19
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