Pub. Date : 2004 Jan 16
PMID : 14741343
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Oxidative refolding of lysozyme in trifluoroethanol (TFE) and ethylene glycol: interfering role of preexisting alpha-helical structure and intermolecular hydrophobic interactions. | Trifluoroethanol | lysozyme | Homo sapiens |
| 2 | Oxidative refolding of lysozyme in trifluoroethanol (TFE) and ethylene glycol: interfering role of preexisting alpha-helical structure and intermolecular hydrophobic interactions. | Trifluoroethanol | lysozyme | Homo sapiens |
| 3 | The oxidative refolding of equilibrium intermediates of lysozyme stabilized in trifluoroethanol (TFE) and ethylene glycol was monitored. | Trifluoroethanol | lysozyme | Homo sapiens |
| 4 | The oxidative refolding of equilibrium intermediates of lysozyme stabilized in trifluoroethanol (TFE) and ethylene glycol was monitored. | Trifluoroethanol | lysozyme | Homo sapiens |
| 5 | Equilibrium intermediates of disulfide reduced lysozyme in TFE are known to contain considerable amounts of alpha-helical structure and resemble the early intermediate in the oxidative refolding of lysozyme. | Trifluoroethanol | lysozyme | Homo sapiens |
| 6 | Equilibrium intermediates of disulfide reduced lysozyme in TFE are known to contain considerable amounts of alpha-helical structure and resemble the early intermediate in the oxidative refolding of lysozyme. | Trifluoroethanol | lysozyme | Homo sapiens |