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Cover Picture: Mechanism of Multivalent Carbohydrate–Protein Interactions Studied by EPR Spectroscopy (Angew. Chem. Int. Ed. 36/2011)
Author(s) -
Braun Patrick,
Nägele Bettina,
Wittmann Valentin,
Drescher Malte
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201104492
Subject(s) - electron paramagnetic resonance , chemistry , divalent , site directed spin labeling , biophysics , crystallography , ligand (biochemistry) , int , chelation , molecule , stereochemistry , biochemistry , nuclear magnetic resonance , receptor , inorganic chemistry , biology , organic chemistry , physics , computer science , operating system , membrane
State‐of‐the‐art EPR techniques provide structural evidence for multivalent protein–ligand interactions in solution. In their Communication page 8428 ff. , V. Wittmann and co‐workers report experiments that give a detailed picture of the molecular mechanism of the binding of divalent ligands to a lectin in solution. Chelating binding is detected directly and can be differentiated from the monovalent binding of multiple molecules.