Surfactants are everywhere in protein science — from biochemical laboratories to industrial detergents. Among them, sodium dodecyl sulfate (SDS) is perhaps the most famous (or infamous), widely used for its ability to bind, deactivate, and often denature proteins. Despite decades of experimental and theoretical work, the molecular details of how surfactants bind to protein surfaces are still not fully understood. In my recent study, “Binding Dynamics of Linear Alkyl-sulfates of Different Chain Lengths on a Protein Surface” [1], I have explored this problem using molecular dynamics (MD) simulations, focusing on how the length of the surfactant’s hydrocarbon chain influences protein binding.