sodium-dodecyl-sulfate and octaethylene-glycol-monotetradecyl-ether

The strong and usually denaturing interaction between anionic surfactants (AS) and proteins/enzymes has both benefits and drawbacks: for example, it is put to good use in electrophoretic mass determinations but limits enzyme efficiency in detergent formulations. Therefore, studies of the interactions between proteins and AS as well as nonionic surfactants (NIS) are of both basic and applied relevance. The AS sodium dodecyl sulfate (SDS) denatures and unfolds globular proteins under most conditions. In contrast, NIS such as octaethylene glycol monododecyl ether (C

Topics: Animals; Cattle; Chickens; Circular Dichroism; Egg Proteins; Ethylene Glycols; Glucosides; Lactalbumin; Lactoglobulins; Micelles; Milk Proteins; Muramidase; Protein Refolding; Protein Unfolding; Scattering, Small Angle; Serum Albumin; Sodium Dodecyl Sulfate; Surface-Active Agents; X-Ray Diffraction