On the thermal stability of the two dimeric forms of ribonuclease A.
- Published Article
- Publication Date
Jul 01, 2005
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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The corresponding record at NLM can be accessed at https://www.ncbi.nlm.nih.gov/pubmed/15950820