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Literature summary extracted from

  • Bucci, E.; Vitagliano, L.; Barone, R.; Sorrentino, S.; D'Alessio, G.; Graziano, G.
    On the thermal stability of the two dimeric forms of ribonuclease A (2005), Biophys. Chem., 116, 89-95.
    View publication on PubMed

General Stability

EC Number General Stability Organism
4.6.1.18 two distinct dimeric forms. In one dimer (AA-CS), the two monmomers swap the C-terminal beta-strand (residues 116-124), while in the other (AA-NS) the two monomers mutually exchange the N-terminal alpha-helix. The two dimers are metastable and dissociate spontaneously to monomers with different kinetics Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.18 Bos taurus P61823
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.6.1.18 pancreas
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 Bos taurus
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Subunits

EC Number Subunits Comment Organism
4.6.1.18 dimer two distinct dimeric forms. In one dimer (AA-CS), the two monmomers swap the C-terminal beta-strand (residues 116-124), while in the other (AA-NS) the two monomers mutually exchange the N-terminal alpha-helix Bos taurus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.6.1.18 additional information
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 two distinct dimeric forms. In one dimer (AA-CS), the two monmomers swap the C-terminal beta-strand (residues 116-124), while in the other (AA-NS) the two monomers mutually exchange the N-terminal alpha-helix. Thermal denaturation of both dimers can be described by a two-step dissociation/unfolding mechanism. The structural determinants for the higher stability of AA-NS should reside in its open interface Bos taurus