Sodium dodecyl sulfate (SDS) is an anionic detergent commonly used in laboratory settings to denature proteins and disrupt cell membranes. It is widely utilized in gel electrophoresis for separating proteins based on their molecular weight.
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SDS binds to proteins and imparts a uniform negative charge, allowing them to be separated by size during electrophoresis.
In SDS-PAGE, SDS is used along with polyacrylamide gel to resolve protein mixtures into individual components.
SDS can lyse cells by disrupting the lipid bilayer of cell membranes, which is useful in DNA and RNA extraction protocols.
It interferes with hydrophobic interactions within proteins, causing them to unfold into linear polypeptide chains.
SDS is often used in conjunction with reducing agents like DTT or β-mercaptoethanol which break disulfide bonds in proteins.
Review Questions
How does SDS contribute to the separation of proteins in gel electrophoresis?
What role does SDS play in cell lysis during nucleic acid extraction?
Why are reducing agents often used alongside SDS in protein studies?
Related terms
Polyacrylamide Gel Electrophoresis (PAGE): A method for separating proteins or nucleic acids based on their size and charge using a polyacrylamide matrix.
Dithiothreitol (DTT): A reducing agent that breaks disulfide bonds within proteins.
β-Mercaptoethanol: A chemical compound used as a reducing agent to disrupt disulfide bonds within proteins.