Sodium dodecyl sulfate-protein polypeptide complexes in 8 M urea with special reference to sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
The effects of 8 M urea on the complexes formed between sodium dodecyl sulfate and protein polypeptide were found to be as follows: (1) The maximum amount of SDS bound is reduced by almost half, and the minimum equilibrium concentration of SDS necessary to reach saturation was nearly doubled; (2) The apparent content of alpha-helical structure deduced from CD measurement is reduced to only 50--70% of that in the presence of sodium dodecyl sulfate alone; (3) The effective size of the sodium dodecyl sulfate-protein polypeptide complex deduced from viscosity measurements is increased, but is still smaller than the effective size of the protein in 8 M urea alone.
D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D010455:Peptides; D011485:Protein Binding; D011489:Protein Denaturation; D011506:Proteins / Q000032:analysis*; D012967:Sodium Dodecyl Sulfate; D014508:Urea; D014783:Viscosity
D010455:Peptides; D011506:Proteins; D012967:Sodium Dodecyl Sulfate; D014508:Urea