| Abstract
| - An amphiphilic homopolymer scaffold has been used to bind to the protein, cytochrome c. This interaction isanalyzed using cyclic voltammetry, native gel electrophoresis, UV−visible absorption, and circular dichroismspectroscopy. The polymer binds to cytochrome c with micromolar affinity and the association of polymer withcytochrome c leads to a structural change of the protein. This conformational change exposes the heme unit of theprotein, which affords an opportunity to reversibly modulate its electron-transfer properties. We have also shown thatthe electrostatic binding of polymer to cytochrome c can be used to disrupt its interaction with its natural partner,cytochrome c peroxidase.
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