Abstract
We have designed β-strand peptides (BP) that stabilize integral membrane proteins (IMP). BPs self-assemble in solution as filaments and become restructured upon association with IMPs; the resulting IMP/BP complexes resist aggregation when diluted in detergent-free buffer and are examined as stable, single particles with low detergent background by electron microscopy. This enables clear visualization of a spectrum of flexible conformations in the highly dynamic ATP-binding cassette (ABC) transporter MsbA.
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