On the folding mechanism of the bacterial outer membrane protein PagP

Membrane proteins represent an important class of macromolecules that play critical roles in many biological processes. The energetic principles underlying their stability, however, are not well understood. To address this deficiency, the kinetics and thermodynamics of the folding of the Escherichia coli outer membrane protein PagP were investigated by exploiting the ability of this polypeptide to refold into detergent micelles and into artificial lipid membranes. Investigations using the latter enabled the contributions to the folding process of both the protein sequence and of the bilayer lipid oomposition to be discerned.