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Literature summary extracted from

  • Pradeep, L.; Shin, H.C.; Scheraga, H.A.
    Correlation of folding kinetics with the number and isomerization states of prolines in three homologous proteins of the RNase family (2006), FEBS Lett., 580, 5029-5032.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.18 Bos taurus
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4.6.1.18 Lithobates pipiens
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Renatured (Commentary)

EC Number Renatured (Comment) Organism
4.6.1.18 comparison of folding kinetics with bovine RNase A and angiogenin at pH 8.0 and 15°C. Direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds via slower phases Lithobates pipiens
4.6.1.18 comparison of folding kinetics with Rana pipiens' onconase and bovine angiogenin at pH 8.0 and 15°C. Direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds via slower phases Bos taurus

Subunits

EC Number Subunits Comment Organism
4.6.1.18 More comparison of folding kinetics with bovine RNase A and angiogenin at pH 8.0 and 15°C. Direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds via slower phases Lithobates pipiens
4.6.1.18 More comparison of folding kinetics with Rana pipiens' onconase and bovine angiogenin at pH 8.0 and 15°C. Direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds via slower phases Bos taurus