文摘
We describe the computational design of a single-chain four-helix bundle that noncovalentlyself-assembles with fully synthetic non-natural porphyrin cofactors. With this strategy, both the electronicstructure of the cofactor as well as its protein environment may be varied to explore and modulate thefunctional and photophysical properties of the assembly. Solution characterization (NMR, UV-vis) of theprotein showed that it bound with high specificity to the desired cofactors, suggesting that a uniquelystructured protein and well-defined site had indeed been created. This provides a genetically expressedsingle-chain protein scaffold that will allow highly facile, flexible, and asymmetric variations to enable selectiveincorporation of different cofactors, surface-immobilization, and introduction of spectroscopic probes.