title: On the thermal stability of the two dimeric forms of ribonuclease A.
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.
authors.affiliation: Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 6, I-80134 Napoli, Italy.
authors.forename: Enrico
authors.initials: E
authors.lastname: Bucci
authors.forename: Luigi
authors.initials: L
authors.lastname: Vitagliano
authors.forename: Roberto
authors.initials: R
authors.lastname: Barone
authors.forename: Salvatore
authors.initials: S
authors.lastname: Sorrentino
authors.forename: Giuseppe
authors.initials: G
authors.lastname: D'Alessio
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Graziano
mesh_terms: 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*
chemical_list: D012259:Ribonuclease, Pancreatic