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Literature summary extracted from

  • Lopez-Alonso, J.P.; Bruix, M.; Font, J.; Ribo, M.; Vilanova, M.; Jimenez, M.A.; Santoro, J.; Gonzalez, C.; Laurents, D.V.
    NMR spectroscopy reveals that RNase A is chiefly denatured in 40% acetic acid: implications for oligomer formation by 3D domain swapping (2010), J. Am. Chem. Soc., 132, 1621-1630.
    View publication on PubMed

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
4.6.1.18 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
4.6.1.18 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

EC Number Organism UniProt Comment Textmining
4.6.1.18 Bos taurus
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-
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Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.18
-
Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.6.1.18 commercial preparation
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Bos taurus
-

Subunits

EC Number Subunits Comment Organism
4.6.1.18 monomer
-
Bos taurus
4.6.1.18 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

EC Number Synonyms Comment Organism
4.6.1.18 ribonuclease A
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Bos taurus
4.6.1.18 RNase A
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Bos taurus