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Updated: Aug 17, 2026

Chemical Triphosphorylation of Oligonucleotides
Published on: June 2, 2022
On the thermal stability of the two dimeric forms of ribonuclease A
Enrico Bucci1, Luigi Vitagliano, Roberto Barone
1Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 6, I-80134 Napoli, Italy.
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.
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