[38] Thermal stability of rhodopsin and opsin in some novel detergents

This chapter reveals that the “ideal” detergent should at least satisfy certain conditions: it should be soluble in a variety of aqueous media over a large range of temperatures, and its perturbance of the protein conformation should be minimal and reversible on reconstitution with lipids.

Abstract

Publisher Summary This chapter compares the stability of rhodopsin and opsin in some promising novel detergents with their stability in a small selection of detergents routinely used in rhodopsin studies. Detergents have proved to be indispensable for structural studies and purification of membrane proteins in the form of mixed protein–detergent micelles and for studies on lipid–protein interaction involving exchange of original lipids for other lipid molecules. This chapter reveals that the “ideal” detergent should at least satisfy certain conditions: (1) it should be soluble in a variety of aqueous media over a large range of temperatures; (2) its perturbance of the protein conformation should be minimal and reversible on reconstitution with lipids; (3) it should be easily removed or exchanged for lipids so as to permit the protein's reconstitution in “artificial” membranes where it can be investigated in an environment closely resembling the natural one; (4) it should be available on a relatively large scale at reasonable costs; and (5) it should be a well-defined, single compound.