Unlocking The Mechanisms: How Sds Denatures Proteins For Effective Analysis
SDS denatures proteins through a multi-step process. First, its hydrophobic tail binds to hydrophobic regions within the protein, disrupting protein interactions. Next, the hydrophilic head group of SDS interacts with water molecules, creating a favorable environment for protein unfolding. This weakens intermolecular forces, causing the protein to unravel. Finally, SDS molecules form micelles, solubilizing the…