Bucci Enrico, Vitagliano Luigi, Barone Roberto, Sorrentino Salvatore, D'Alessio Giuseppe, Graziano Giuseppe
Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 6, I-80134 Napoli, Italy.
Biophys Chem. 2005 Jul 1;116(2):89-95. doi: 10.1016/j.bpc.2005.03.002. Epub 2005 Apr 7.
The thermal stability of the two dimers of RNase A with N- or C-terminal swapped ends is investigated by means of dissociation kinetics, differential scanning calorimetry, and circular dichroism measurements. The data indicate that the dimer characterized by the swapping of the N-terminal alpha-helices is less prone to monomerize when compared to the dimer characterized by the swapping of the C-terminal beta-strands. This finding is correlated to the structural features of the so-called open interface of the dimeric forms.
通过解离动力学、差示扫描量热法和圆二色性测量，研究了核糖核酸酶A（RNase A）两种N端或C端互换的二聚体的热稳定性。数据表明，与以C端β链互换为特征的二聚体相比，以N端α螺旋互换为特征的二聚体不太容易单体化。这一发现与二聚体形式的所谓开放界面的结构特征相关。
