Abstract
Assignment of NMR resonance frequencies to a particular atom in the molecule establishes a vital step for any detailed structural study. Approaches for sequential assignment typically involve amide proton detection, which may become suboptimal in case of intrinsically disordered proteins (IDPs) at high pH and/or temperature. Here we describe an alternative approach: assignment protocol based on alpha proton detected triple-resonance experiments, which offer several advantages over well-established experiments relying on amide proton detection. Our experiments are suitable for studies of IDPs at any pH and enable sequential assignment of proline-rich segments.
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Acknowledgment
We thank Elina Ahovuo for excellent technical assistance. This work was supported by the grants 122170 and 131144 (to P.P.) from the Academy of Finland.
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Permi, P., Hellman, M. (2012). Alpha Proton Detection Based Backbone Assignment of Intrinsically Disordered Proteins. In: Uversky, V., Dunker, A. (eds) Intrinsically Disordered Protein Analysis. Methods in Molecular Biology, vol 895. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-927-3_15
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DOI: https://doi.org/10.1007/978-1-61779-927-3_15
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