What Is the Mechanism of SDS Binding to Proteins?
The mechanism of SDS binding to proteins involves both hydrophobic and electrostatic interactions. SDS is a cationic surfactant with a long hydrophobic hydrocarbon tail and a negatively charged sulfate head. Due to its amphipathic nature, SDS can interact with many biomolecules, including proteins.
The hydrophobic tail of SDS interacts with the hydrophobic amino acid residues of the protein, unfolding its three-dimensional structure into a linear or near-linear form. This is crucial in SDS-PAGE, as it ensures that protein samples are primarily separated based on molecular weight rather than their complex 3D structure. The sulfate head of SDS carries a negative charge, so when SDS binds to the protein, it imparts a negative charge to the protein. This causes the protein to be separated in SDS-PAGE mainly according to its size, rather than its original charge.
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