Silk proteins are natural polymers which are synthesized by insects like silkworms and spiders. There are two proteins in the silk obtained from the cocoon of B. mori, these are silk fibroin and silk sericin. While the silk fibroin is the main part of the cocoon with a high commercial importance, sericin is the “glue” protein that holds fibroins together. Sericin has wide variety of applications from cosmetics to biomaterial research. Because of its high fibrillar structure, it can be used in wound healing or drug delivery studies. It can be obtained from the degumming process of cocoons which includes chemical treatment like alkali treatment and boiling, or biological treatment like enzymatic digestion. However, sericin obtained by these processes are not consistent in structure, and the sequence of the protein obtained depends on the extraction methodology and conditions. However, proteins obtained by recombinant production can be standardized, and repeat-chain length can be adjusted as desired. In this thesis study, a sericin like protein which includes eight repeats of the 38 amino acid sequence of the natural sericin was cloned and expressed in E. coli. The resulting protein, Ser-8mer, was analyzed in terms of fibril structure and secondary structure. It was found out that the protein has beta sheet conformation in contrast to commercial sericin with random coils. And as a result of this conformation, it forms insoluble self-assembled fibril structures which shows a promising contribution to the biomaterial research.