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Chaperone proteins

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Chaperone proteins

Postby ryanbarnhill » Wed Feb 24, 2010 6:50 pm

Can anyone tell what portion of a protein chaperones bind?
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Re: Chaperone proteins

Postby Swede » Wed Feb 24, 2010 8:12 pm

I think chaparons bind to hydrophobic parts of proteins, no matter the aa-sequence, folding it correctly. I'm not too sure thought.
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Postby JackBean » Wed Feb 24, 2010 8:36 pm

The are several types of chaperons, some can bind just short part of polypeptide (e.g. after translation or during transport through membrane) or they can bind whole protein inside (as GroEL-GroES system)
http://www.biolib.cz/en/main/

Cis or trans? That's what matters.
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Postby AndrewPhD » Thu Feb 25, 2010 2:37 am

ive always understood it as the chaperonin create a hydrophobic area to act as a "safe-haven' for the denatured proteins to renature.
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Postby MrMistery » Wed Mar 03, 2010 10:19 pm

@andrew
some of them do, like the GroEL-GroES complex. But there are other kind of chaperones. Proteins like Kar2 and Hrd3 seem to be able to bind any exposed hydrophobic segments, but they are nowhere near as elaborate as Gro
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