The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization.

@article{Schlapschy2004ThePE,
  title={The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization.},
  author={Martin Schlapschy and Monica K Dommel and Kamyar Hadian and Marton Fogarasi and Ingo P Kornd{\"o}rfer and Arne Skerra},
  journal={Biological chemistry},
  year={2004},
  volume={385 2},
  pages={137-43}
}
The 'seventeen kilodalton protein' Skp confers transient solubility on outer membrane proteins during biogenesis in Gram-negative bacteria. Here we report a first biophysical characterization of this chaperone itself, which also possesses biotechnological potential in the production of recombinant proteins. Using cross-linking and gel filtration methods, we found that Skp forms a stable homo-trimer in solution. Following thermal denaturation, monitored by CD spectroscopy, this chaperone refolds… CONTINUE READING