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A more recent version of this article appeared on August 24, 2001
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Papers In Press, published online ahead of print June 29, 2001
J. Biol. Chem, 10.1074/jbc.R100031200
Submitted on May 11, 2001
Revised on June 22, 2001
Accepted on June 29, 2001

Detergents as tools in membrane biochemistry

R. Michael Garavito and Shelagh Ferguson-Miller

Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824-1319

Corresponding Author: garavito{at}msu.edu

Detergents are invaluable tools for studying membrane proteins. However, these deceptively simple, amphipathic molecules exhibit complex behavior when they self-associate and interact with other molecules. The phase behavior and assembled structures of detergents are markedly influenced not only by their unique chemical and physical properties, but also by concentration, ionic conditions and the presence of other lipids and proteins. In this minireview, we discuss the various aggregate forms detergents assume and some misconceptions about their structure. The distinction between detergents and the membrane lipids that they may (or may not) replace, is emphasized in the most recent high-resolution structures of membrane proteins. Detergents are clearly friends and foes, but with the knowledge of how they work, we can use the increasing variety of detergents to our advantage.


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