Abstract
Determining hydrogen exchange kinetics in proteins can shed light on their structure and dynamics. Nuclear magnetic resonance (NMR) spectroscopy is an important analytical technique to determine exchange rates. In this chapter, we describe a new method (Paris-DÉCOR) to determine fast protein amide backbone hydrogen exchange rates in the range 10 to 104 s−1. Measuring fast exchange rates is particularly important for the study of intrinsically disordered proteins, where there is very little protection from exchange to the solvent by the formation of persistent structure. We provide a protocol to set up the experiment as well as MATLAB scripts for numerical simulation that is needed to determine the exchange rates.
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Acknowledgments
This work was supported by a postdoctoral fellowship to R.D. from the VILLUM Foundation.
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Dass, R., Mulder, F.A.A. (2020). Paris-DÉCOR: A Protocol for the Determination of Fast Protein Backbone Amide Hydrogen Exchange Rates. In: Kragelund, B.B., Skriver, K. (eds) Intrinsically Disordered Proteins. Methods in Molecular Biology, vol 2141. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0524-0_17
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DOI: https://doi.org/10.1007/978-1-0716-0524-0_17
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Publisher Name: Humana, New York, NY
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