Organic Solvent | Comment | Organism |
---|---|---|
additional information | The conformation of ribonuclease A in 40% acetic acid is found to be mostly but not completely unfolded. All X-Pro bonds are predominantly in the trans conformation and the hydrophobic core and the beta-sheet structure unfold completely. However, three alpha-helices are partly populated in ribonuclease A in 40% acetic acid in approximately the same positions as the three native helices. | Bos taurus |
urea | no helical structure is found in 8 M urea at pH 2.5, ribonuclease A can oligomerize after thorough unfolding in concentrated solutions of urea, followed by a gel filtration step, which exchanges the denaturant for a refolding buffer. The yield of ribonuclease A oligomers depends on the logarithm of ribonuclease A concentration during refolding. | Bos taurus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Bos taurus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Bos taurus | - |
Subunits | Comment | Organism |
---|---|---|
monomer | - |
Bos taurus |
oligomer | ribonuclease A can form a series of 3D domain swapped oligomers by exchanging the N-terminal alpha-helix or the C-terminal beta-strand or both. These oligomers have additional biological and enzymatic activities that the monomeric protein lacks. Ribonuclease A oligomerization is induced by 40% acetic acid, which has been assumed to mildly unfold the protein by detaching the terminal segments and consequently facilitating intersubunit swapping, once the acetic acid is removed by lyophilization and the protein is redissolved in a benign buffer | Bos taurus |
Synonyms | Comment | Organism |
---|---|---|
ribonuclease A | - |
Bos taurus |
RNase A | - |
Bos taurus |