## Abstract A novel process has been developed which uses reversed micelles to isolate denatured protein molecules from each other and allows them to refold individually. These reversed micelles are aqueous phase droplets stabilized by the surfactant AOT and suspended in isoβoctane. By adjusting co
Protein refolding in reversed micelles
β Scribed by Anna J. Hagen; T. Alan Hatton; Daniel I. C. Wang
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 1016 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0006-3592
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A novel process has been developed to improve the refolding yield of denatured proteins. It uses reversed micelles to isolate denatured protein molecules from each other and thus, upon refolding, reduces the intermolecular interactions which lead to aggregation. The feasibility of this process was f
This article reports that a reversed micellar solution is useful for refolding proteins directly from a solid source. The solubilization of denatured RNase A, which had been prepared by reprecipitation from the denaturant protein solution, into reversed micelles formulated with sodium di-2-ethylhexy