Structures of Glycans Bound to Receptors from Saturation Transfer Difference (STD) NMR Spectroscopy: Quantitative Analysis by Using CORCEMA-ST

Enríquez-Navas, Pedro M., Guzzi, Cinzia, Muñoz-García, Juan C., Nieto, Pedro M. and Angulo, Jesus ORCID: https://orcid.org/0000-0001-7250-5639 (2015) Structures of Glycans Bound to Receptors from Saturation Transfer Difference (STD) NMR Spectroscopy: Quantitative Analysis by Using CORCEMA-ST. In: Glycoinformatics. Methods in Molecular Biology, 1273 (1). Springer (Humana Press), pp. 475-487. ISBN 978-1-4939-2342-7

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Abstract

Glycan–receptor interactions are of fundamental relevance for a large number of biological processes, and their kinetics properties (medium/weak binding affinities) 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.

Item Type:	Book Section
Faculty \ School:	Faculty of Science > School of Pharmacy (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Drug Delivery and Pharmaceutical Materials (former - to 2017) Faculty of Science > Research Groups > Pharmaceutical Materials and Soft Matter
Depositing User:	Pure Connector
Date Deposited:	09 Mar 2015 09:40
Last Modified:	25 Sep 2024 10:40
URI:	https://ueaeprints.uea.ac.uk/id/eprint/52565
DOI:	10.1007/978-1-4939-2343-4_28

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