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J. Biol. Chem., Vol. 276, Issue 35, 32403-32406, August 31, 2001
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and
From the Department of Biochemistry and Molecular Biology,
Michigan State University, East Lansing, Michigan 48824-1319
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.
This minireview is dedicated to Drs. Jacqueline A. Reynolds and the late Martin Zulauf who gave one of us (R. M. G.) invaluable insights into the behavior of detergents.
To whom correspondence may be addressed. Tel.: 517-355-9724; Fax:
517-353-9334; E-mail: garavito@msu.edu.
§
To whom correspondence may be addressed. Tel.: 517-355-0199; Fax:
517-353-9334; E-mail: fergus20@msu.edu.
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