D153G |
shift of maximum luminescence to shorter wavelengths. t1/2 is decreased with respect to the half-life time of the native protein (0.7 s). Mutation results in a significant decrease in stability at 65°C |
Aequorea victoria |
W86F |
shift of maximum luminescence to shorter wavelengths. The single mutant reaches the highest stability against thermal shock |
Aequorea victoria |
W86F/D153G |
decreased t1/2-value. Maximum emission spectrum at 401 nm. Mutation results in a significant decrease in stability at 65°C |
Aequorea victoria |
Y82F |
mutation shifts the peak towards longer wavelengths. Increased half time of initial light by 3.6 s. Mutation results in a significant decrease in stability at 65°C |
Aequorea victoria |
Y82F/D153G |
decreased t1/2-value. Maximum emission spectrum at 478 nm |
Aequorea victoria |
Y82F/W86F |
maximum emission spectrum at 400 nm. Y82F mutation results in shift of emission to longer wavelength, while the W86F mutation shifts the emission to shorter wavelengths. Compared to wild type aequorin, the Y82F/W86F variant displays a 2fold increase of light half-life. Mutation results in a significant decrease in stability at 65°C |
Aequorea victoria |