1b:I[76749,["/_next/static/chunks/bf18fea59be6d5b1.js","/_next/static/chunks/1ba21a8e081e29d1.js","/_next/static/chunks/0383663887945ae7.js","/_next/static/chunks/2060b26370dc6c0a.js","/_next/static/chunks/c89b4435b8c37fcf.js","/_next/static/chunks/8ddf2550f38c2f2a.js","/_next/static/chunks/5bf36002c846d2d8.js"],"default"] 1c:I[3486,["/_next/static/chunks/bf18fea59be6d5b1.js","/_next/static/chunks/1ba21a8e081e29d1.js","/_next/static/chunks/0383663887945ae7.js","/_next/static/chunks/2060b26370dc6c0a.js","/_next/static/chunks/c89b4435b8c37fcf.js","/_next/static/chunks/8ddf2550f38c2f2a.js","/_next/static/chunks/5bf36002c846d2d8.js"],"default"] 1d:I[17707,["/_next/static/chunks/bf18fea59be6d5b1.js","/_next/static/chunks/1ba21a8e081e29d1.js","/_next/static/chunks/0383663887945ae7.js","/_next/static/chunks/2060b26370dc6c0a.js","/_next/static/chunks/c89b4435b8c37fcf.js","/_next/static/chunks/8ddf2550f38c2f2a.js","/_next/static/chunks/5bf36002c846d2d8.js"],"default"] 1e:I[66528,["/_next/static/chunks/bf18fea59be6d5b1.js","/_next/static/chunks/1ba21a8e081e29d1.js","/_next/static/chunks/0383663887945ae7.js","/_next/static/chunks/2060b26370dc6c0a.js","/_next/static/chunks/c89b4435b8c37fcf.js","/_next/static/chunks/8ddf2550f38c2f2a.js","/_next/static/chunks/5bf36002c846d2d8.js"],"default"] 1f:I[63176,["/_next/static/chunks/bf18fea59be6d5b1.js","/_next/static/chunks/1ba21a8e081e29d1.js","/_next/static/chunks/0383663887945ae7.js","/_next/static/chunks/2060b26370dc6c0a.js","/_next/static/chunks/c89b4435b8c37fcf.js","/_next/static/chunks/8ddf2550f38c2f2a.js","/_next/static/chunks/5bf36002c846d2d8.js"],"default"] 20:I[87099,["/_next/static/chunks/bf18fea59be6d5b1.js","/_next/static/chunks/1ba21a8e081e29d1.js","/_next/static/chunks/0383663887945ae7.js","/_next/static/chunks/2060b26370dc6c0a.js","/_next/static/chunks/c89b4435b8c37fcf.js","/_next/static/chunks/8ddf2550f38c2f2a.js","/_next/static/chunks/5bf36002c846d2d8.js"],"default"] 21:I[26200,["/_next/static/chunks/bf18fea59be6d5b1.js","/_next/static/chunks/1ba21a8e081e29d1.js","/_next/static/chunks/0383663887945ae7.js","/_next/static/chunks/2060b26370dc6c0a.js","/_next/static/chunks/c89b4435b8c37fcf.js","/_next/static/chunks/8ddf2550f38c2f2a.js","/_next/static/chunks/5bf36002c846d2d8.js"],"Group"] 22:I[23365,["/_next/static/chunks/bf18fea59be6d5b1.js","/_next/static/chunks/1ba21a8e081e29d1.js","/_next/static/chunks/0383663887945ae7.js","/_next/static/chunks/2060b26370dc6c0a.js","/_next/static/chunks/c89b4435b8c37fcf.js","/_next/static/chunks/8ddf2550f38c2f2a.js","/_next/static/chunks/5bf36002c846d2d8.js"],"default"] 23:T417,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.

Shengcao Shi

Publications