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.
ON THE THERMAL STABILITY OF THE TWO DIMERIC FORMS OF RIBONUCLEASE A / D'Alessio, Giuseppe; Sorrentino, Salvatore; Bucci, E; Vitagliano, L; Barone, ; Graziano, G.. - In: BIOPHYSICAL CHEMISTRY. - ISSN 0301-4622. - STAMPA. - 116:(2005), pp. 89-95.
ON THE THERMAL STABILITY OF THE TWO DIMERIC FORMS OF RIBONUCLEASE A.
D'ALESSIO, GIUSEPPE;SORRENTINO, SALVATORE;
2005
Abstract
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.| File | Dimensione | Formato | |
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