Speaker
Description
The structural color change of cephalopods is primarily driven by the self-assembly of reflectin proteins, which modulates the refractive index of the Bragg reflection layer, thereby altering the propagation of light. Additionally, when induced by small molecules like imidazole, reflectin will undergo higher-order assembly, forming a hexagonal lamellar structure. This work employs small-angle neutron scattering (SANS), quasi-elastic neutron scattering (QENS), and neutron spin-echo (NSE) techniques to investigate the structural and dynamic changes in reflectin assembly. Specifically, we examined the effects of temperature, sample concentration, and small molecules on the self-assembly process of reflectin.
After analysis, we found that: i) As the temperature increases, the structure of the protein becomes more compact, while all its dynamic motions are enhanced. ii) As the protein concentration increases, the protein structure becomes more compact. The addition of imidazole prevents the protein structure from becoming more compact as concentration increases. iii) The addition of imidazole enhances large-scale spatial motions while suppressing small-scale spatial motions. The enhancement in dynamics at large scale is attributed to the larger-scale motions associated with the high-order self-assembly of reflectin. The results will contribute to establishing a more precise and well-defined mechanism of reflectin self-assembly at the molecular level, providing a theoretical foundation for advancing applications of this color-changing behavior.
