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)

Research output: Chapter in Book/Report/Conference proceedingChapter

6 Citations (Scopus)


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 languageEnglish
Title of host publicationGlycoinformatics
EditorsThomas Lütteke, Martin Frank
PublisherSpringer (Humana Press)
ISBN (Electronic)978-1-4939-2343-4
ISBN (Print)978-1-4939-2342-7
Publication statusPublished - 2015

Publication series

NameMethods in Molecular Biology
PublisherHumana Press
ISSN (Print)1064-3745

Cite this