QUESTIONS: alpha-helix "signals" in proteins

Sarah Tilley sjt at newt.phys.unsw.edu.au
Sun Jul 17 22:28:11 EST 1994


-- 
**
In article <2vhv54$i94 at news.doit.wisc.edu>, kenp at banyo (Kenneth Prehoda) writes:

[stuff deleted]
|
|>Also, as far as I know chaperones are simply catalysts and do not
|>affect the end state of protein folding.  The final native state
|>will be the same whether or not a chaperone is present - albeit
|>it much more slowly without.
|>
|
|>-Ken Prehoda
|>kenp at nmrfam.wisc.edu
|>

At the risk of seeming too pedantic, I would like to point out that there are many different types of chaperone available in the cell. While some enzymes catalyse protein folding, I am fairly sure that proteins under the classification of chaperone don't. They appear to act by preventing the formation of 'incorrect' structures which may lead to misfolding or aggregation. The final native state is the same with or without a chaperone present, but in the case of bacterial chaperonin60 there are examples wher

e refolding in the presence of chaperonin are slower than spontaneous refolding.

(for a review see Gething and Sambrook, Nature, 355, 33-45, 1992)

Sarah Tilley



More information about the Proteins mailing list