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H/D exchange of a 15 N labelled Tau fragment as measured by a simple Relax-EXSY experiment

Abstract : We present an equilibrium H/D exchange experiment to measure the exchange rates of labile amide protons in intrinsically unfolded proteins. By measuring the contribution of the H/D exchange to the apparent T1 relaxation rates in solvents of different D2O content, we can easily derive the rates of exchange for rapidly exchanging amide protons. The method does not require double isotope labelling, is sensitive, and requires limited fitting of the data. We demonstrate it on a functional fragment of Tau, and provide evidence for the hydrogen bond formation of the phosphate moiety of Ser214 with its own amide proton in the same fragment phosphorylated by the PKA kinase.
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https://hal.univ-lille.fr/hal-03235804
Contributeur : Lilloa Université de Lille <>
Soumis le : mercredi 26 mai 2021 - 08:40:41
Dernière modification le : jeudi 27 mai 2021 - 03:35:32

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Juan Lopez, Puneet Ahuja, Isabelle Landrieu, Francois-Xavier Cantrelle, Isabelle Huvent, et al.. H/D exchange of a 15 N labelled Tau fragment as measured by a simple Relax-EXSY experiment. Journal of Magnetic Resonance, Elsevier, 2014, Journal of Magnetic Resonance, 249, pp.32-37. ⟨10.1016/j.jmr.2014.10.008⟩. ⟨hal-03235804⟩

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