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Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy

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Book cover Protein-Carbohydrate Interactions

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1588))

Abstract

Solution-state nuclear magnetic resonance (NMR) spectroscopy can be used to monitor protein-carbohydrate interactions. Two-dimensional 1H-15N heteronuclear single quantum coherence (HSQC)-based techniques described in this chapter can be used quickly and effectively to screen a set of possible carbohydrate binding partners, to quantify the dissociation constant (K d) of any identified interactions, and to map the carbohydrate binding site on the structure of the protein. Here, we describe the titration of a family 32 carbohydrate binding module from Clostridium perfringens (CpCBM32) with the monosaccharide N-acetylgalactosamine (GalNAc), in which we calculate the apparent dissociation of the interaction, and map the GalNAc binding site onto the structure of CpCBM32.

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Correspondence to Julie M. Grondin .

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Grondin, J.M., Langelaan, D.N., Smith, S.P. (2017). Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy. In: Abbott, D., Lammerts van Bueren, A. (eds) Protein-Carbohydrate Interactions. Methods in Molecular Biology, vol 1588. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6899-2_11

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  • DOI: https://doi.org/10.1007/978-1-4939-6899-2_11

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-6898-5

  • Online ISBN: 978-1-4939-6899-2

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