J. Buchner, M. Schmidt, M. Fuchs, R. Jaenicke, R. Rudolph, F.X. Schmid, T. Kiefhaber, "GroE facilitates refolding of citrate synthase by suppressing aggregation," Biochemistry, 30:1591-94, 1991.
Johannes Buchner (Institut fr Biophysik und Physikalische Biochemie, Universitat Regensburg, Germany) and Thomas Kiefhaber (Stanford University, California): "Folding and unfolding reactions in the cell are assisted by a set of helper proteins called molecular chaperones. Of these chaperones, two proteins from E. coli bacterium--GroEL and GroES--are the best studied.
"Although several models have been proposed for their mode of action, there has been no direct experimental validation. We used spectroscopic techniques, and we used light scattering in particular, to directly determine the effect of GroE on protein folding in vitro.
"We showed that aggregation of citrate synthase, which completes with proper folding, can be suppressed completely in the presence of GroEL.
"Furthermore, we demonstrated that the GroE system is not able to dissolve already ...
