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- URN to cite this document:
- urn:nbn:de:bvb:355-epub-341846
- DOI to cite this document:
- 10.5283/epub.34184
Alternative links to fulltext:DOI
Abstract
The native state of a globular protein is essential for its biocatalytic function, but is marginally stable against unfolding. While unfolding equilibria are often reversible, folding intermediates and misfolds can promote irreversible protein aggregation into amorphous precipitates or highly ordered amyloid states. Addition of ionic liquids—low-melting organic salts—offers intriguing prospects ...
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