Previous work on the partial digestion of the native and denatured forms of tRNASer and tRNAPhe from yeast with TI-RNAase was extended. Detailed studies with pancreatic and T2-RNAase and a few experiments with sheep kidney nuclease and acid RNAase from hog spleen revealed characteristically different fragmentation patterns for the native and denatured forms of the tRNAs. Apparently it is mainly the miniloop and dihydrouridine regions which are involved in the conformational changes responsible for denaturation.The rate constants, activation enthalpies, and activation entropies of the renaturation process were calculated from amino acid acceptance data.When the changes in hyperchromicity a t 260 nm of the denatured tRNAs were followed as a function of time, a process was detected which in tRNAPhe is 5-10 times and in tRNAser 10-20 times faster than the renaturation as measured by acceptor activity. The whole net change in absorption, possibly representing the total net change in base stacking, occurs during the fast, process. The activation enthalpies and activation entropies are different for the fast and t,he over-all processes.