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Binding Epitopes of Gangliosides to their Neuronal Receptor, Myelin‐Associated Glycoprotein, from Saturation Transfer Difference NMR
Author(s) -
Shin SoYoung,
Gäthje Heiko,
Schwardt Oliver,
Gao GanPan,
Ernst Beat,
Kelm Soerge,
Meyer Bernd
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800485
Subject(s) - epitope , tetrasaccharide , glycoprotein , heteronuclear single quantum coherence spectroscopy , chemistry , saturation (graph theory) , biochemistry , computational biology , stereochemistry , biology , two dimensional nuclear magnetic resonance spectroscopy , immunology , antibody , mathematics , combinatorics , polysaccharide
MAGnificent analysis to remove ambiguity : The binding epitopes of tri‐ and tetrasaccharide ligands in their interactions with the myelin‐associated glycoprotein (MAG) have been studied by using saturation transfer difference NMR, in which the signal intensities can help to resolve overlapped HSQC signals. In the figure, the signals of the protons with the closest proximity to the protein are shown in red (30–60 %) or blue (61–100 %).