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

Pedro M. Enríquez-Navas; Cinzia Guzzi; Juan C.  Muñoz-García; Pedro M. Nieto; Jesus Angulo

doi:10.1007/978-1-4939-2343-4_28

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

Pedro M. Enríquez-Navas, Cinzia Guzzi, Juan C. Muñoz-García, Pedro M. Nieto, Jesus Angulo (Lead Author)

Pharmaceutical Materials and Soft Matter

Research output: Chapter in Book/Report/Conference proceeding › Chapter

6 Citations (Scopus)

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.

Original language	English
Title of host publication	Glycoinformatics
Editors	Thomas Lütteke, Martin Frank
Publisher	Springer (Humana Press)
Pages	475-487
Volume	1273
Edition	1
ISBN (Electronic)	978-1-4939-2343-4
ISBN (Print)	978-1-4939-2342-7
DOIs	https://doi.org/10.1007/978-1-4939-2343-4_28
Publication status	Published - 2015

Publication series

Name	Methods in Molecular Biology
Publisher	Humana Press
Volume	1273
ISSN (Print)	1064-3745

Access to Document

10.1007/978-1-4939-2343-4_28

Cite this

Enríquez-Navas, PM., 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. In T. Lütteke, & M. Frank (Eds.), Glycoinformatics (1 ed., Vol. 1273, pp. 475-487). (Methods in Molecular Biology; Vol. 1273). Springer (Humana Press). https://doi.org/10.1007/978-1-4939-2343-4_28

Enríquez-Navas, Pedro M. ; Guzzi, Cinzia ; Muñoz-García, Juan C. et al. / Structures of Glycans Bound to Receptors from Saturation Transfer Difference (STD) NMR Spectroscopy: Quantitative Analysis by Using CORCEMA-ST. Glycoinformatics. editor / Thomas Lütteke ; Martin Frank. Vol. 1273 1. ed. Springer (Humana Press), 2015. pp. 475-487 (Methods in Molecular Biology).

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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 STDNMR 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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Enríquez-Navas, PM, Guzzi, C, Muñoz-García, JC, Nieto, PM & Angulo, J 2015, Structures of Glycans Bound to Receptors from Saturation Transfer Difference (STD) NMR Spectroscopy: Quantitative Analysis by Using CORCEMA-ST. in T Lütteke & M Frank (eds), Glycoinformatics. 1 edn, vol. 1273, Methods in Molecular Biology, vol. 1273, Springer (Humana Press), pp. 475-487. https://doi.org/10.1007/978-1-4939-2343-4_28

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. et al.

Glycoinformatics. ed. / Thomas Lütteke; Martin Frank. Vol. 1273 1. ed. Springer (Humana Press), 2015. p. 475-487 (Methods in Molecular Biology; Vol. 1273).

Research output: Chapter in Book/Report/Conference proceeding › Chapter

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Enríquez-Navas PM, Guzzi C, Muñoz-García JC, Nieto PM, Angulo J. Structures of Glycans Bound to Receptors from Saturation Transfer Difference (STD) NMR Spectroscopy: Quantitative Analysis by Using CORCEMA-ST. In Lütteke T, Frank M, editors, Glycoinformatics. 1 ed. Vol. 1273. Springer (Humana Press). 2015. p. 475-487. (Methods in Molecular Biology). doi: 10.1007/978-1-4939-2343-4_28