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b-barrel membrane proteins in Gram-negative bacteria, mitochondria, and chloroplasts are assembled by highly conserved multi-protein complexes. The mechanism by which these molecular machines fold and insert their substrates is poorly understood. It has not been possible to dissect the folding and insertion pathway because the process has not been reproduced in a biochemical system.
We purified the components that fold and insert Escherichia coli outer membrane proteins and reconstituted b-barrel protein assembly in proteoliposomes using the enzymatic activity of a protein.

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