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Biophysical Journal 61: 1435-1439 (1992)
© 1992 the Biophysical Society

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Protein structures in SDS micelle-protein complexes.

W Parker and P S Song

Department of Chemistry, University of Nebraska, Lincoln 68588-0304.

ABSTRACT

Sodium dodecyl sulfate (SDS) is used more often than any other detergent as an excellent denaturing or "unfolding" detergent. However, formation of ordered structure (alpha-helix or beta-sheet) in certain peptides is known to be induced by interaction with SDS micelles. The SDS-induced structures formed by these peptides are amphiphilic, having both a hydrophobic and a hydrophilic face. Previous work in this area has revealed that SDS induces helical folding in a wide variety of non-helical proteins. Here, we describe the interaction of several structurally unrelated proteins with SDS micelles and the correlation of these structures to helical amphiphilic regions present in the primary sequence. It is likely that the ability of native nonordered protein structures to form induced amphiphilic ordered structures is rather common.






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Copyright © 1992 by the Biophysical Society.