Abstract
A protein undergoes a variety of structural changes during its folding and misfolding and a knowledge of its behaviour is key to understanding the molecular details of these events. Solution-state NMR spectroscopy is unique in that it can provide both structural and dynamical information at both high-resolution and at a residue-specific level, and is particularly useful in the study of dynamic systems. In this chapter, we describe NMR strategies and how they are applied in the study of protein folding and misfolding.
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Acknowledgements
We would like to thank the members of the Christodoulou lab for useful discussions and Dr. John Kirkpatrick for critical reading of this chapter.
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Cabrita, L.D., Waudby, C.A., Dobson, C.M., Christodoulou, J. (2011). Solution-State Nuclear Magnetic Resonance Spectroscopy and Protein Folding. In: Hill, A., Barnham, K., Bottomley, S., Cappai, R. (eds) Protein Folding, Misfolding, and Disease. Methods in Molecular Biology, vol 752. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60327-223-0_7
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