On the thermal stability of the two dimeric forms of ribonuclease A.
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.
Bucci
Enrico
E
Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 6, I-80134 Napoli, Italy.
Vitagliano
Luigi
L
Barone
Roberto
R
Sorrentino
Salvatore
S
D'Alessio
Giuseppe
G
Graziano
Giuseppe
G
D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D002942:Circular Dichroism; D019281:Dimerization; D004795:Enzyme Stability; D006358:Hot Temperature; D007700:Kinetics; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*
D012259:Ribonuclease, Pancreatic