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Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE)
. When protein molecules are treated with SDS, the detergent disrupts the secondary, tertiary, and quaternary structure to produce linear polypeptide chains coated with negatively charged SDS molecules.
. The detergent binds to hydrophobic regions of the denatured protein chain in a constant ratio of about 1.4 g of SDS per gram of protein.
The presence of mercaptoethanol assists in protein denaturation by reducing all disulfide bonds.
If protein samples are treated so that they have a uniform charge, electrophoretic
mobility then depends only on size.
. Thus, the molecular weights of proteins may be estimated if they are subjected to electrophoresis in the presence of a detergent, sodium dodecyl sulfate (SDS), and a disulfide bond reducing agent, mercaptoethanol.
Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE)
. When protein molecules are treated with SDS, the detergent disrupts the secondary, tertiary, and quaternary structure to produce linear polypeptide chains coated with negatively charged SDS molecules.
. The detergent binds to hydrophobic regions of the denatured protein chain in a constant ratio of about 1.4 g of SDS per gram of protein.
The presence of mercaptoethanol assists in protein denaturation by reducing all disulfide bonds.
If protein samples are treated so that they have a uniform charge, electrophoretic
mobility then depends only on size.
. Thus, the molecular weights of proteins may be estimated if they are subjected to electrophoresis in the presence of a detergent, sodium dodecyl sulfate (SDS), and a disulfide bond reducing agent, mercaptoethanol.
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