Detalle de: Structures of Glycans Bound to Receptors from Saturation Transfer Difference (STD) NMR Spectroscopy: Quantitative Analysis by Using CORCEMA-ST
| Title | Structures of Glycans Bound to Receptors from Saturation Transfer Difference (STD) NMR Spectroscopy: Quantitative Analysis by Using CORCEMA-ST |
| 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. |
| Apa Reference | 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, 475-487. 10.1007/978-1-4939-2343-4_28 |
| Doi | 10.1007/978-1-4939-2343-4_28 |
| Publication Date | 2015 |
| Publication Type | Book / chapter |
| Researcher | Juan Carlos Muñoz García |
| Ontology | Experimental structure determination, Molecular flexibility, Molecular Interactions/Docking |
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