Protein folding GroEL

How does the GroEL-GroES complex function as a chaperone to assist protein folding Although several aspects of the mechanism are not clear, the main features of the functional cycle are known. The first step is the... [Pg.102]

Enzymes assist formation of proper disulfide bonds during folding Isomerization of proline residues can be a rate-limiting step in protein folding Proteins can fold or unfold inside chaperonins GroEL is a cylindrical structure with a... [Pg.414]

Langer, T., Lu., C, Echols, H., Flanagan, J, Hayer, M.K., Hartl, F.-U. (1992). Successive action of Dnak, DnaJ, GroEL along the pathway of chaperone mediated protein folding. Nature 356, 683-689. [Pg.456]

Sigler PB, Xu Z, Rye HS, Burston SG, Fenton WA, Horwich AL (1998) Structure and function in GroEL-mediated protein folding. Annu Rev Biochem 67 581-608 Silberman JD, Sogin ML, Leipe DD, Clark CG (1996) Human parasite finds taxonomic home. Nature 380 398... [Pg.299]

ALLOSTERY AND PROTEIN SUBSTRATE CONFORMATIONAL CHANGE DURING GroEL/GroES-MEDIATED PROTEIN FOLDING... [Pg.45]

Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., and Hard, F. U. (1991). Chaperonin-mediated protein folding at the surface of groEL through a molten globule -like intermediate. Nature 352, 36-42. [Pg.386]

Mayhew, M., da Silva, A. C., Martin, J., Erdjument-Bromage, H., Tempst, P., and Hard, F. U. (1996). Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature 379, 420-426. [Pg.386]

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