Glycan-receptor interactions are of fundamental relevance for a large number of biological processes, and their kinetics properties (medium/weak binding affi nities) make them appropriated to be studied by ligand observed NMR techniques, among which saturation transfer difference (STD) NMR spectroscopy has been shown to be a very robust and powerful approach. The quantitative analysis of the results from a STD NMR study of a glycan-receptor interaction is essential to be able to translate the resulting spectral intensities into a 3D molecular model of the complex. This chapter describes how to carry out such a quantitative analysis by means of the Complete Relaxation and Conformational Exchange Matrix Approach for STD NMR (CORCEMA-ST), in general terms, and an example of a previous work on an antibody-glycan interaction is also shown.
CITATION STYLE
Enríquez-Navas, P. M., Guzzi, C., Muñoz-García, J. C., Nieto, P. M., & Angulo, J. (2015). Structures of glycans bound to receptors from saturation transfer difference (STD) NMR spectroscopy: Quantitative analysis by using CORCEMA-ST. Methods in Molecular Biology, 1273, 475–487. https://doi.org/10.1007/978-1-4939-2343-4_28
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