A tetrameric protein dissociates into dimers when the detergent sodium dodecyl sulfate (SDS) is added to a solution of the protein. But the dimers are termed SDS-resistant because they do not further dissociate into monomers in the presence of the detergent. What intermolecular forces might be acting at the dimer-dimer interface? Are the intermolecular forces acting at the monomer-monomer interface different? Explain.
Proteins are polymers of amino acids linked by peptide bonds. Proteins can be single chain or more than one chain. Tetrameric protein contains four polypeptide chains.
Detergent SDS (Sodium dodecyl sulfate) is an anionic surfactant which is used as protein denaturating agent in the laboratory. It works by disrupting the non-covalent bonds (like hydrophobic interactions and hydrogen bonds) in the proteins which causes loss in the native conformations and shapes of protein molecules. SDS binds to proteins at a ratio of one SDS molecule per 2 amino acid residues. Negatively charged SDS detergent provides all proteins with uniform negative charge with similar charge-to-mass ratio which is useful for the separation of protein based on it molecular weight.
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