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.
On the thermal stability of the two dimeric forms of ribonuclease A
Bucci Enrico;Vitagliano Luigi;
2005
Abstract
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.File in questo prodotto:
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