J. Martin, T. Langer, R. Boteva, A. Schramel, A.L. Horwich, F.-U. Hartl, "Chaperonin-mediated protein folding at the surface of groEL through a `molten globule'-like intermediate," Nature, 352:36-42, 1991.
F.-Ulrich Hartl (Memorial Sloan Kettering Cancer Center, New York): "Molecular chaperones, proteins that help other proteins to fold, have emerged over recent years as an important topic of research in biology. While their physiological significance has been established through a combination of genetic and cell biological methodology, little was known about how these fascinating proteins function at the molecular level.
"In this paper, we analyzed the major chaperone protein of the bacterium Escherichia coli, groEL, and its partner protein, groES. An in vitro system was established in which groEL and groES mediate the ATP-dependent folding of denatured substrate proteins.
"This approach allowed the dissection of the chaperone-dependent folding reaction into distinct steps. We could show that groEL, a doughnut-shaped complex of 800 ...
