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GroEL proteins mechanism

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]

The complex mechanism shown in Figure 19.23 summarizes these steps. In addition, some proteins may need to be sequestered inside the cage-like structure of GroEL, which can probably accommodate proteins up to 70 kDa.88 The... [Pg.316]

Proposed molecular mechanism of GroEL-facilitated reconstitution of oligomeric proteins. Many aspects in this figure such as roles of GroES (chaperonin-10) and ATP remain unclear. See text for details. [Pg.68]

H. lones, M. Preuss, M. Wright and A. D. MiUer, The mechanism of GroEL/GroES folding/refolding of protein substrates revisited, Org. Biomol. Chem., 2006,4,1223-1235. [Pg.549]

Horwich, Arthur, Horwich Laboratory Web Site, Yale University. Available online URL http //info.med.yale.edu/genetics/horwich/. Accessed April 3, 2006. This site describes a mechanism for protein folding by the GroEL/GroES chaperone system. [Pg.403]

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See also in sourсe #XX -- [ Pg.64 , Pg.65 ]



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