The formation of protein gel networks in aqueous systems is a result of protein intermolecular interactions after an energy input, like heating. In this research, we report that a redox reaction between Au3+ions and proteins can also lead to the formation of a protein gel network. Amino acids, like cysteine and tyrosine, get oxidized and form covalent bonds with neighboring protein molecules, while Au3+ions get reduced to Au+and Au0, nucleate and form gold nanoparticles. The protein gel network formation occurs within 2 h at room temperature and can be tuned by varying Au3+/protein ratio and accelerated by increasing the incubation temperature. The proposed Au3+-induced gel network formation was applied to different proteins, like egg yolk high-density lipoprotein, bovine serum albumin and whey protein. This research opens new insights for the investigation of the metal-protein interactions and may aid in the design of novel hybrid-soft nanocomposite materials.