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Origins of Molecular Chaperones ?

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Origins of Molecular Chaperones ?

Postby cloudnine » Sat Jan 01, 2005 5:00 am

Hello everyone, please tell me what may be the answer.

In protein synthesis, the functional protein is the one with the correct folding pattern.
This is aided by the special proteins called chaperones.
In this case, when these proteins were first synthesized, what is the assisting factors to fold them to function as chaperones?
Is that concerned with maternal genes, or the genes products from mother?
if not, what is meant by correct folding of proteins?
Or what is the command for the first folding of the first protein of life?

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Postby thank.darwin » Fri Feb 11, 2005 2:15 pm

I can't help you with all of your questions but I will give you some information about the folding of a protein... Proteins fold because bonds, such as a hydrogen bond, form between the proteins. It all has to do with the remainder group of the protein.
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Postby DevGrp » Fri Feb 11, 2005 3:26 pm

many proteins will fold themselves naturally without chaperones.. Gently denature them in a tube, remove the denaturing chemical conditions and they will fold back the way they were.
It is also todo with them finding the best / most stable favoured molecular configuration.

My understanding is that chaperones help protein fold into less favoured configurations which they would not normally fold into without the chaperone.

So the chaperone can probably fold itself and without the chaperone the chaperoned protein would find some other configuration which may well be either inactive / unstable / less active.

hope this helps
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Postby RobJim » Sat Feb 19, 2005 4:40 am

Are you asking this question from an evolutionary perspective? This seems like the kind of question proponents of 'irreduceable complexity' might ask.
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