Conformational Change of Protein/SDS Complex in Low Ionic Strength Solution — A Study by Dynamic Light Scattering
Proteins are macromolecules which contain a polypeptide backbone (strongly hydrophilic) and many side chains which are generally hydrophobic. In order to minimize its energy a protein molecule in an aqueous solution tends to form a globular structure which buries as many hydrophobic side chains in the interior as possible. But a complete removal of the hydrophobic side chains from their contact with water is impossible and these hydrophobic patches (if sufficiently large) can constitute some binding sites for other hydrocarbon or amphiphilic molecules. The detergents are known to be good protein denaturing agents. When these detergent molecules attach themselves to the binding sites and neutralize the hydrophobic effect, it becomes energetically favorable for some new interior hydrophobic side chains to expose themselves to the water molecules and thus form some new binding sites. This kind of cooperative effect has been discussed by Reynolds and Tanford.1
KeywordsSodium Dodecyl Sulfate Dynamic Light Scattering Critical Micellar Concentration Hydrophobic Effect Globular Structure
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