Renaturation of the brain myelin proteins by octyl glucoside detergent

The secondary structure of myelin proteins undergoes a deep change when the membrane is delipidated and suspended in an aqueous buffer containing phosphate and sulfate anions. However, when increasing concentrations of octyl glucoside are dissolved in this saline medium, proteins recover gradually its native secondary structure, reaching a maximum for a detergent/protein ratio which, in addition, is optimal for maximal membrane solubilization. Larger amounts of detergent, however, reverted the effect. Results are explained in terms of anion-lipid and detergent-lipid interactions. Quantitative estimates on the spectral profiles let us find the optimal detergent-protein stoichiometry for preserving almost completely the native secondary structure of myelin proteins while keeping maximal solubilization. These findings are of great importance for reconstitution experiments designed with the goal of determining the biological functions of myelin proteins.