Pub. Date : 2010 Feb 10
PMID : 20085318
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | NMR spectroscopy reveals that RNase A is chiefly denatured in 40% acetic acid: implications for oligomer formation by 3D domain swapping. | Acetic Acid | ribonuclease A family member 1, pancreatic | Homo sapiens |
| 2 | RNase 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. | Acetic Acid | ribonuclease A family member 1, pancreatic | Homo sapiens |
| 3 | RNase 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. | Acetic Acid | ribonuclease A family member 1, pancreatic | Homo sapiens |
| 4 | Using UV difference, near UV circular dichroism, folding kinetics, and multidimensional heteronuclear NMR spectroscopy, the conformation of RNase A in 40% acetic acid and in 8 M urea has been characterized. | Acetic Acid | ribonuclease A family member 1, pancreatic | Homo sapiens |
| 5 | These studies demonstrate that RNase A is chiefly unfolded in 40% acetic acid; it partially retains the native helices, whereas the beta-sheet is fully denatured and all X-Pro peptide bonds are predominantly in the trans conformation. | Acetic Acid | ribonuclease A family member 1, pancreatic | Homo sapiens |