Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands,Angewandte Chemie International Edition

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Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands
Angewandte Chemie International Edition ( IF 16.1 ) Pub Date : 2017-07-19 07:45:29 , DOI: 10.1002/anie.201707041
Guang Yang ₁ , Hong-ming Ding ₂ , Zdravko Kochovski ₃ , Rongting Hu ₁ , Yan Lu _{3,

4} , Yu-qiang Ma _{2,

5} , Guosong Chen ₁ , Ming Jiang ₁

Affiliation

In nature, proteins are organized into highly ordered self-assembled structures with various morphologies and dimensions. In their Communication (DOI: 10.1002/anie.201703052), Y. Ma, G. Chen, and co-workers report the fabrication of protein assemblies by using native protein LecA as a building block through sugar–protein interactions and rhodamine dimerization. The morphologies and dimensions of the protein assemblies can be controlled by the length of the tether between the sugar and rhodamine.

中文翻译：

由组装诱导配体的系链长度调节的天然蛋白质到1D，2D和3D结构的高度有序的自组装

在自然界中，蛋白质被组织成具有各种形态和尺寸的高度有序的自组装结构。Y. Ma，G. Chen及其同事在其交流（DOI：10.1002 / anie.201703052）中报告了通过使用天然蛋白质LecA作为糖-蛋白质相互作用和若丹明二聚化的结构单元来制造蛋白质组装体的过程。蛋白质组装体的形态和尺寸可以通过糖和若丹明之间的系链长度来控制。

更新日期：2017-07-20

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