GroEL 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... 

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... 

Chymotrypsinogen 480, 481 Chymotrypsin inhibitor 2 (CI2) folding kinetics 544-577, 577 GroEL binding 605 fragments 577, 578, 587, 588, 595 mechanism of folding 576-588 structure 576, 577 Circular dichroism (CD) 193-195 optimal absorbance for signal to noise 212-214... 

The essence of the mechanism of GroEL is first to prevent hydrophobic folding intermediates from sticking to one another and then, when necessary, to allow a... 

Fiqurc 19 21 Annealing mechanism for GroEL. A misfolded state that does not fold productively is formed more rapidly from the initial unfolded state (U) than the correctly folded state (N) is formed. Unfolding the misfolded state (annealing) allows further attempts at productive folding. At each attempt, the proportion of N... 

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. 

Figure 2 Mechanism of action of the GroEL/GroES system in E.coli. P, unfolded polypeptide chain. N, native folded chain. For details, see text. Reprinted from Reference (16), Copyright 2003 with permission from Elsevier.

Weissman, J. S., Hohl, C. M., Kovalenko, O., Kashi, Y., Chen, S., Braig, K, Saibil, H. R., Fenton, W. A., and Horwich, A. L. (1995). Mechanism of GroEL action Productive release of polypeptide from a sequestered position under GroES. Cell 83, 577-587. 

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