On the thermal stability of the two dimeric forms of ribonuclease A

The thermostability of the 2 dimers of RNase A with N- or C-terminal swapped ends was investigated by means of dissocn. kinetics, DSC, and CD measurements. The data indicated that the dimer characterized by the swapping of the N-terminal a-helixes was less prone to monomerize when compared to the dimer characterized by the swapping of the C-terminal b-strands. This finding was correlated to the structural features of the so-called open interface of the dimeric forms.