Abstract
CPMG relaxation dispersion NMR experiments have emerged as a powerful method to characterize protein minor states that are in exchange with a visible dominant conformation, and have lifetimes between ~0.5 and 5 milliseconds (ms) and populations greater than 0.5%. The structure of the minor state can, in favorable cases, be determined from the parameters provided by the CPMG relaxation dispersion experiments. Here, we go through the intricacies of setting up these powerful CPMG experiments.
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Acknowledgments
DFH and PV are grateful to Prof. Lewis E Kay (University of Toronto), Dr. Ranjith Muhandiram, Dr. Algirdas Velyvis, Dr. Dmitry Korzhnev, Dr. Vitali Tugarinov, Dr. Philipp Neudecker, Dr. Patrik Lundstrom, and other members of the Kay lab who exposed them to many of the methods presented here. DFH acknowledges the Biotechnology and Biological Sciences Research Council UK (BBSRC) for financial support. PV is supported by generous startup grant from TCIS/TIFH.
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Gopalan, A.B., Hansen, D.F., Vallurupalli, P. (2018). CPMG Experiments for Protein Minor Conformer Structure Determination. In: Ghose, R. (eds) Protein NMR. Methods in Molecular Biology, vol 1688. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7386-6_11
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DOI: https://doi.org/10.1007/978-1-4939-7386-6_11
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