How does (sodium dodecyl sulfate) SDS denature a protein?
Posted June 22, 2020
Answer
SDS is an amphiphilic molecule that has both hydrophilic group and hydrophobic group. Once SDS is added to a protein solution, it can interact with both the hydrophilic and hydrophobic side-chain groups. Since the 3D structure of a protein is mainly held together by hydrophobic interactions and hydrogen bonds between the side chains, the addition of SDS can interfere with both, resulting in the unfolding and denaturation.
Additional resources
Amplite™ Fluorimetric Fluorescamine Protein Quantitation Kit *Blue Fluorescence*
Amplite™ Rapid Colorimetric Total Protein Thiol Quantitation Assay Kit
Branden, C. I., & Tooze, J. (2012). Introduction to protein structure. Garland Science.