Institut Curie, U1006 INSERM, 26 rue d'Ulm, 75005 Paris, France.
Nano Lett. 2011 Sep 14;11(9):3983-6. doi: 10.1021/nl202351t. Epub 2011 Aug 3.
The capacity of proteins to carry out different functions is related to their ability to undergo conformation changes, which depends on the flexibility of protein structures. In this work, we applied a novel imaging mode based on indentation force spectroscopy to map quantitatively the flexibility of individual membrane proteins in their native, folded state at unprecedented submolecular resolution. Our results enabled us to correlate protein flexibility with crystal structure and showed that α-helices are stiff structures that may contribute importantly to the mechanical stability of membrane proteins, while interhelical loops appeared more flexible, allowing conformational changes related to function.
蛋白质执行不同功能的能力与其构象变化的能力有关，而这又取决于蛋白质结构的灵活性。在这项工作中，我们应用了一种基于压痕力谱的新型成像模式，以前所未有的亚分子分辨率定量绘制了天然折叠状态下单个膜蛋白的柔韧性。我们的结果使我们能够将蛋白质的柔韧性与晶体结构相关联，并表明α-螺旋是僵硬的结构，可能对膜蛋白的机械稳定性有重要贡献，而螺旋间环则更加灵活，允许与功能相关的构象变化。
