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Aleuria aurantia Agglutinin Recognizes Multiple Conformations of α‐ L ‐Fuc‐(1→6)‐β‐ D ‐GlcNAc‐OMe
Author(s) -
Weimar Thomas,
Peters Thomas
Publication year - 1994
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199400881
Subject(s) - chemistry , fucose , stereochemistry , residue (chemistry) , agglutinin , disaccharide , lectin , biochemistry , glycoprotein
A significant preference for the (1 → 6) linkage , but not for a particular conformation with regard to this bond is shown by the agglutinin from Aleuria aurantia when it binds to carbohydrates with the fucose residue. This is revealed by NMR spectroscopic studies on the rather flexible disaccharide 1 , which showed that at least members of two major conformational families, gg and gt , are bound.