Mechanism of protein denaturation by SDS

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This research combines two areas of study - protein/detergent interactions and protein folding. Certain kinds of detergents called ionic detergents are very effective at binding to proteins. This strong binding changes the shape of the protein, and because proteins are normally tightly folded up into precise 3D shapes, these strongly binding detergents unfold the protein. This usually destroys the function of the protein, but the detergent-unfolded state can be used in many protein biotechnology applications. For example, one of the most widely used analytical methods in biochemistry labs is to measure the molecular weight of detergent-unfolded proteins by electrophoresis. Despite the common use of detergents in these applications, we do not know how ionic detergents bind to proteins. One of the goals of this research is to understand how and why these detergents bind so strongly to proteins. On a second front, my lab has discovered a simple way to change the protein binding properties of ionic detergents. With this method, we can convert a strongly binding detergent into a weakly binding detergent. The weakly binding form of the detergent does not unfold protein, and this method has potential applications in the production of folded protein that cannot be obtained by other methods. Our investigations into the fundamental mechanism of detergent binding to proteins may lead to improved methods for producing protein in the biotechnology and the pharmaceutical industries.