Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro.

@article{Burgess2008BetabarrelPT,
  title={Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro.},
  author={Nancy K Burgess and Thuy Phuong Dao and Ann Marie Stanley and Karen G Fleming},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 39},
  pages={26748-58}
}
Little is known about the dynamic process of membrane protein folding, and few models exist to explore it. In this study we doubled the number of Escherichia coli outer membrane proteins (OMPs) for which folding into lipid bilayers has been systematically investigated. We cloned, expressed, and folded nine OMPs: outer membrane protein X (OmpX), OmpW, OmpA, the crcA gene product (PagP), OmpT, outer membrane phospholipase A (OmpLa), the fadl gene product (FadL), the yaet gene product (Omp85), and… CONTINUE READING

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