Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.
 

Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.

Related Articles Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.

Methods Mol Biol. 2017;1588:143-156

Authors: Grondin JM, Langelaan DN, Smith SP

Abstract
Solution-state nuclear magnetic resonance (NMR) spectroscopy can be used to monitor protein-carbohydrate interactions. Two-dimensional (1)H-(15)N 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.


PMID: 28417366 [PubMed - in process]



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