Activation of Calcineurin Involves a Folding Upon Binding Event

Abstract

developing in vitro lipid bicelle and bilayer folding systems for membrane proteins. Bicelle properties, as well as the stored curvature elastic stress of model bilayers can be used to optimise the rate, yield and stability of folded protein. We have shown that events such as transmembrane helix insertion, as well as tertiary and quaternary structure formation are altered by the stored curvature stress of the bilayer. Either changing the lipid chains or introducing a different headgroup such as phosphoethanolamine alters the curvature stress of a phosphatoidylcholine lipid bilayer. Our results on a variety of monomeric, multidomain and multi-subunit proteins will be described.