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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.
Julie M Grondin, and
David N Langelaan, and
Steven P Smith
January 1998,
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Julie M Grondin, and
David N Langelaan, and
Steven P Smith
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Julie M Grondin, and
David N Langelaan, and
Steven P Smith
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Julie M Grondin, and
David N Langelaan, and
Steven P Smith
March 2023,
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Julie M Grondin, and
David N Langelaan, and
Steven P Smith
May 2017,
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Julie M Grondin, and
David N Langelaan, and
Steven P Smith
November 2004,
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Julie M Grondin, and
David N Langelaan, and
Steven P Smith
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Julie M Grondin, and
David N Langelaan, and
Steven P Smith
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Julie M Grondin, and
David N Langelaan, and
Steven P Smith
January 2002,
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Julie M Grondin, and
David N Langelaan, and
Steven P Smith
January 2006,
Trends in biotechnology,
