Protein structural changes induced by their uptake at interfaces

Abstract

For insertion into lipidic media, most hydrosoluble proteins must cross the lipid–water interface and thus undergo conformational transitions. According to their chemical sequences these transitions may be restricted to changes involving only the tertiary structure, while for other proteins this environment modification will induce drastic changes such as the unfolding of large domains. The structural transitions are mainly governed by the presence of hydrophobic domains and/or by the existence of induced amphipathic properties.