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Silk proteins are of great interest to the scientific community owing to their unique mechanical properties and interesting biological functionality. In addition, the silk proteins are not burned out following heating, rather they are transformed into a carbonaceous solid, pyroprotein; several studies have identified potential carbon precursors for state-of-the-art technologies. However, no mechanism for the carbonization of proteins has yet been reported. Here we examine the structural and chemical changes of silk proteins systematically at temperatures above the onset of thermal degradation. We find that the beta-sheet structure is transformed into an sp²-hybridized carbon hexagonal structure by simple heating to 350 ºC. The pseudographitic crystalline layers grew to form highly ordered graphitic structures following further heating to 2,800 C. Our results provide a mechanism for the thermal transition of the protein and demonstrate a potential strategy for designing pyroproteins using a clean system with a catalyst-free aqueous wet process for various applications. In particular, they have a great potential in alkali ion storage. Several different types of pyroprotein-derived carbon materials and their electrochemical performances will be introduced with the basic alkali ion storage mechanism of conventional carbon materials.