Literature summary for 4.6.1.18 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.

Search for more literature for 4.6.1.18

General Stability

General Stability	Organism
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

Organism	UniProt	Comment	Textmining
Bos taurus	P61823	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
pancreas	-	Bos taurus	-

Subunits

Subunits	Comment	Organism
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]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	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

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Release 2023.1 (January 2023)