Proteins have a large number of biochemical functions. Stability of the proteins is dependent on certain conditions, including temperature, pH and ionic strength. They work only in a narrow range of temperature. When protein is heated to a specific temperature, there will be changes in its secondary, tertiary, and quaternary structure, which is called denaturation. This behavior causes changes in the functional properties of protein. There are many studies about thermal properties of the proteins in the literature [1-3]. But, there is no report about thermal properties of proteininorganic hybrid nanoflowers yet. Flower-mimicking nanostructures have attracted considerable interest in recent years [4-6]. Integrating biomolecules (proteins, DNA etc) as functional building blocks into the inorganic nanoflowers further offers a tool to modulate their nanostructures. This approach confers specific biological activities to facilitate their applications in various fields [7]. In this study, flower-like hybrid protein-inorganic structures were synthesized using a common protein (bovine serum albumine, BSA) and metal ions (Cu2+) at different pHs and different protein concentrations. The structures that were created by the assemby of nano-sized leaf-shaped structures with the formation of bond are called flower-like nanostructure because of the resulting structure resembles a flower. These synthesized hybrid nanoflowers were characterized using SEM, EDX, FTIR analysis. Also, the thermal behavior such as glass transition and crystallization of protein-inorganic hybrid nanoflowers was investigated in detail using differential scanning calorimetry (DSC), TGA.