Chapter title |
Structures of Glycans Bound to Receptors from Saturation Transfer Difference (STD) NMR Spectroscopy: Quantitative Analysis by using CORCEMA-ST
|
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Chapter number | 28 |
Book title |
Glycoinformatics
|
Published in |
Methods in molecular biology, February 2015
|
DOI | 10.1007/978-1-4939-2343-4_28 |
Pubmed ID | |
Book ISBNs |
978-1-4939-2342-7, 978-1-4939-2343-4
|
Authors |
Pedro M Enríquez-Navas, Cinzia Guzzi, Juan C Muñoz-García, P.M. Nieto, Jesús Angulo, Pedro M. Enríquez-Navas, Juan C. Muñoz-García, Pedro M. Nieto |
Editors |
Thomas Lütteke, Martin Frank |
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. |
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