title: Refolding of SDS-denatured proteins using amphipathic cosolvents and osmolytes.
abstract: Currently, the investigation of protein refolding processes involves several time-consuming 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.
authors.affiliation: Department of Chemistry, Unité de Chimie Physique Théorique et Structurale, University of Namur, Namur, Belgium.
authors.forename: Guillaume
authors.initials: G
authors.lastname: Roussel
authors.forename: Emmanuel
authors.initials: E
authors.lastname: Tinti
authors.forename: Eric
authors.initials: E
authors.lastname: Perpète
authors.forename: Catherine
authors.initials: C
authors.lastname: Michaux
mesh_terms: D003902:Detergents / Q000737:chemistry*; D057075:Enzyme Assays; D006018:Glycols / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry*; D009994:Osmolar Concentration; D011489:Protein Denaturation; D020673:Protein Renaturation; D011506:Proteins / Q000737:chemistry; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry*; D012996:Solutions; D012997:Solvents / Q000737:chemistry
chemical_list: D003902:Detergents; D006018:Glycols; D011506:Proteins; D012996:Solutions; D012997:Solvents; D012967:Sodium Dodecyl Sulfate; D009113:Muramidase; C011480:hexylene glycol