A study of protein-sodium dodecyl sulfate complexes by transient electric birefringence.
The method of transient electric birefringence has been applied to study the conformation of protein-sodium dodecyl sulfate complexes. A model of a deformable prolate ellipsoid has been proposed for the protein-dodecyl sulfate complex. This model is compared to the models proposed by J. A. Reynolds and C. Tanford (1970), J. Biol. Chem. 245, 5161) and K. Shirahama, K. Tsujii, and T. Takagi (1974, J. Biochem. 75, 309). Differences between these latter two models are resolved by the model presented here. In addition, it has been demonstrated that protein molecular weights may be obtained from the slow relaxation time for transient electric birefringence of protein-dodecyl sulfate complexes.
D000818:Animals; D001665:Binding Sites; D001718:Birefringence; D002417:Cattle; D002919:Chymotrypsinogen; D003574:Cytochrome c Group; D006801:Humans; D007700:Kinetics; D007782:Lactoglobulins; D008722:Methods; D008970:Molecular Weight; D009113:Muramidase; D010047:Ovalbumin; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins; D012710:Serum Albumin, Bovine; D012967:Sodium Dodecyl Sulfate; D013997:Time Factors; D014168:Transferrin
D003574:Cytochrome c Group; D007782:Lactoglobulins; D011506:Proteins; D014168:Transferrin; D012710:Serum Albumin, Bovine; D012967:Sodium Dodecyl Sulfate; D010047:Ovalbumin; D002919:Chymotrypsinogen; D009113:Muramidase