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Single Amino Acid Exchange in Bacteriophage HK620 Tailspike Protein Results in Thousand Fold Increase of its Oligosaccharide Affinity

机译:噬菌体中的单氨基酸交换HK620尾磷蛋白质导致其寡糖亲和力的千倍增加

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摘要

Although of great importance for biological recognition processes, driving forces for carbohydrate protein complex formation are still elusive. Understanding thermodynamics of interactions between amphiphilic protein and sugar molecules in aqueous solution however would be important for binding site predictions. We have established a model system from bacteriophage tailspike proteins (TSP) recognizing bacterial outer membrane polysaccharides to study structural thermodynamics of large carbohydrate complexes (1-3).
机译:虽然对生物识别过程非常重要,但碳水化合物蛋白复杂形成的驱动力仍然难以捉摸。然而了解水溶液中两亲蛋白质和糖分子之间的相互作用的热力学对结合位点预测是重要的。我们已经建立了一种来自噬菌体尾剂蛋白(TSP)的模型系统,识别细菌外膜多糖,以研究大型碳水化合物复合物的结构热力学(1-3)。

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