beta-Barrel proteins from bacterial outer membranes: structure, function and refolding

Recently solved outer membrane protein structures include the smallest and largest known beta-barrel structures, with functions distinct from the gene ral and specific porins. Both protein expressed in outer membranes and prot ein deposited as cytoplasmic aggregates have been used for the structure de terminations. As most beta-barrel proteins can be overexpressed in an aggre gated form (inclusion bodies) and refolded to the native state, this provid es an alternative to membrane-targeted expression strategies and yields suf ficient quantities of protein for future structural studies.