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Abstract
Currently, the investigation of protein refolding processes involves several timeconsuming stages that require large amounts of protein and costly chemicals. Consequently, there is great interest in developing new approaches to the study of protein renaturation that are more technically and economically feasible. It has recently been reported that certain cosolvents are able to modulate the denaturing properties of sodium dodecyl sulfate (SDS) and induce the refolding of proteins. This unit presents a protocol to study and follow the renaturation of a protein (membrane or soluble) starting from a native or SDS-unfolded state using a variety of candidate cosolvents and osmolytes.
Original language | English |
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Article number | 28.5 |
Pages (from-to) | 1 - 9 |
Number of pages | 9 |
Journal | Current Protocols in Protein Science |
Volume | 28.5 |
Issue number | SUPPL.72 |
DOIs | |
Publication status | Published - 3 Sept 2013 |
Keywords
- Cosolvent
- Osmolyte
- Protein refolding
- Sodium dodecyl sulfate
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Dive into the research topics of 'Refolding of SDS-denatured proteins using amphipathic cosolvents and osmolytes'. Together they form a unique fingerprint.Projects
- 1 Finished
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Folding studies and characterization of membrane proteins.
ROUSSEL, G. (PI), Michaux, C. (CoI) & Perpete, E. (CoI)
1/10/10 → 1/10/14
Project: PHD