力谱学
锌
半胱氨酸
化学
锌指
结晶学
原子力显微镜
结合位点
生物物理学
螺旋束
分子
蛋白质折叠
蛋白质结构
金属
纳米技术
生物化学
材料科学
生物
有机化学
酶
基因
转录因子
作者
Ziyi Wang,Jingyuan Nie,Shengcao Shi,Guoqiang Li,Peng Zheng
摘要
α3D is a de novo designed three-helix bundle protein. Like most naturally occurring helical proteins, it is mechanically labile with an unfolding force of <15 pN, revealed by atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS). This protein has been further designed with a tri-cysteine metal-binding site, named α3DIV, which can bind heavy transition metals. Here, we demonstrate that incorporating such a metal-binding site can transform this mechanically labile protein into a stable one. We show that zinc binds to the tri-cysteine site and increases the unfolding force to ∼160 pN. This force is one order of magnitude higher than that of the apo-protein (<15 pN). Moreover, the unfolding mechanism of Zn-α3DIV indicates the correct zinc binding with the tri-cysteine site, forming three mechanostable Zn-thiolate bonds. Thus, α3DIV could be a potential α-helical structure-based building block for synthesizing biomaterials with tunable mechanical properties.
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