Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California, USA.
Nat Methods. 2012 Oct;9(10):981-4. doi: 10.1038/nmeth.2175. Epub 2012 Sep 16.
The reversible covalent attachment of chemical probes to proteins has long been sought as a means to visualize and manipulate proteins. Here we demonstrate the full reversibility of post-translational custom pantetheine modification of Escherichia coli acyl carrier protein for visualization and functional studies. We use this iterative enzymatic methodology in vitro to reversibly label acyl carrier protein variants and apply these tools to NMR structural studies of protein-substrate interactions.
长期以来，人们一直寻求将化学探针可逆地共价连接到蛋白质上，作为可视化和操作蛋白质的一种手段。在这里，我们证明了大肠杆菌酰基辅酶 A 载体蛋白的翻译后定制泛酰巯基乙胺修饰的完全可逆性，用于可视化和功能研究。我们在体外使用这种迭代酶促方法可逆地标记酰基辅酶 A 载体蛋白变体，并将这些工具应用于蛋白质-底物相互作用的 NMR 结构研究。
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