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On the thermal stability of the two dimeric forms of ribonuclease A.

Authors
Type
Published Article
Journal
Biophysical Chemistry
0301-4622
Publisher
Elsevier
Publication Date
Volume
116
Issue
2
Pages
89–95
Identifiers
PMID: 15950820
Source
Medline
License
Unknown

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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