Articles | Volume 2, issue 1
Research article
01 Jul 2021
Research article |  | 01 Jul 2021

Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues

Isabella C. Felli, Wolfgang Bermel, and Roberta Pierattelli

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Field: Liquid-state NMR | Topic: Pulse-sequence development
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Cited articles

Ahuja, P., Cantrelle, F. X., Huvent, I., Hanoulle, X., Lopez, J., Smet, C., Wieruszeski, J. M., Landrieu, I., and Lippens, G.: Proline conformation in a functional Tau fragment, J. Mol. Biol., 428, 79–91,, 2016. 
Alik, A., Bouguechtouli, C., Julien, M., Bermel, W., Ghouil, R., Zinn-Justin, S., and Theillet, F. X.: Sensitivity-Enhanced 13C-NMR spectroscopy for monitoring multisite phosphorylation at physiological temperature and pH, Angew. Chem. Int. Edit., 59, 10411–10415,, 2020. 
Bermel, W., Bertini, I., Felli, I. C., Kümmerle, R., and Pierattelli, R.: Novel 13C direct detection experiments, including extension to the third dimension, to perform the complete assignment of proteins, J. Magn. Reson., 178, 56–64,, 2006a. 
Bermel, W., Bertini, I., Felli, I. C., Lee, Y.-M., Luchinat, C., and Pierattelli, R.: Protonless NMR experiments for sequence-specific assignment of backbone nuclei in unfolded proteins, J. Am. Chem. Soc., 128, 3918–3919,, 2006b. 
Bermel, W., Bertini, I., Csizmok, V., Felli, I. C., Pierattelli, R., and Tompa, P.: H-start for exclusively heteronuclear NMR spectroscopy: The case of intrinsically disordered proteins, J. Magn. Reson., 198, 275–281,, 2009. 
Short summary
NMR represents a key spectroscopic technique for studying intrinsically disordered proteins (IDPs) that lack a stable three-dimensional structure. We present a set of NMR experiments tailored for proline residues, which are highly abundant in IDPs. The novel experiments have very interesting properties for the investigation of IDPs of increasing complexity.