Dry ribonuclease was irradiated with 60Co gamma radiation in vacuo, under oxygen atmosphere, and at 77 °K. By chromatography on Sephadex G-50 active ribonuclease was separated from inactive radiation products. From the elution pattern and by ultracentrifugation it was shown that mainly unfolded dimers are formed by gamma irradiation of dry ribonuclease. Amino acid analysis of these various products shows that in all components cystine, methionine, tyrosine, phenylalanine, lysine, and histidine are destroyed with increasing dose whereas glycine shows a small increase. Thus, in ribonuclease irradiated in the dry state the same amino acids are changed as was found after irradiation in aqueous solutions. The radiosensitivity of dry ribonuclease shows an increase by the presence of oxygen of about 2 and a decrease at low temperature in vacuo of about 5. The same factors were also found for the alteration of amino acids, which means that under various experimental conditions amino acid destruction is proportional to loss of enzymatic activity of ribonuclease. The observed selectivity of amino acid destruction may be explained by energy migration or by the attack of atomic hydrogen liberated at random from the molecule. The total number of amino acids destroyed per ribonuclease molecule increases with dose. In enzymatically inactive products this value is always higher by one amino acid residue than in the active components. From this result and from the increase with dose it is concluded that after destruction of one amino acid residue the ribonuclease molecule has a probability (not depending on dose of irradiation) of 0.45 to become inactivated whereas in 55 per cent of all cases the molecule maintains its enzymatic activity.