We have compared the effect of microwave irradiation and of conventional heating on the fluorescence of solution-based green fluorescent protein. A specialized near-field 8.5 GHz microwave applicator operating at 250 mW input microwave power was used. The solution temperature, the intensity, and the spectrum of the green fluorescent protein fluorescence 1), under microwave irradiation and 2), under conventional heating, were measured. In both cases the fluorescence intensity decreases and the spectrum becomes red-shifted. Although the microwave irradiation heats the solution, the microwave-induced changes in fluorescence cannot be explained by heating alone. Several possible scenarios are discussed.

The mechanisms of amino acids synthesis behind high temperature shock-waves were elucidated and distinction was made between the steps occurring in the gas phase and those occurring in solution. In the presence of water vapor, aldehydes and HCN are formed separately in regions of different temperatures along the reacting gas. The aldehydes and ammonia condense to aldimines which add HCN to form alpha-amino nitriles, all in the gas phase. The hydrolysis to amino acids takes place in solution. In the absence of water vapor, aldimines and HCN are formed in the gas phase but condense to alpha-amino nitriles only in solution. A fair amount of oxygen only lowers the production of amino acids, which consequently could be still produced in the presence of oxygen in the Earth's primitive atmoshere. The waterless mechanism can operate in the Jovian atmosphere and supply it with ample amounts of amino acids, especially aspartic.