Cover Picture: Mechanism of Multivalent Carbohydrate–Protein Interactions Studied by EPR Spectroscopy (Angew. Chem. Int. Ed. 36/2011)
Cover Picture: Mechanism of Multivalent Carbohydrate–Protein Interactions Studied by EPR Spectroscopy (Angew. Chem. Int. Ed. 36/2011)
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封面图片：通过 EPR 光谱研究多价碳水化合物与蛋白质相互作用的机制（Angew Chem Int Ed 36/2011）
DOI：
10.1002/anie.201104492
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发表时间：
2011
影响因子：
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通讯作者：
M. Drescher
中科院分区：
文献类型：
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作者：
P. Braun;B. Nägele;V. Wittmann;M. Drescher
最先进的EPR技术为溶液中多价蛋白质-配体相互作用提供了结构证据。在其通信页8428 ff.中，V. Wittmann及其同事报告了实验，该实验详细描述了二价配体与溶液中凝集素结合的分子机制。螯合结合可直接检测，并可与多个分子的单价结合区分开来。
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.