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Topic: protein folding  (Read 7223 times)

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Zami87

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protein folding
« on: May 24, 2005, 07:56:22 AM »
I have some questions about chaperonins and protein folding...
1.How do chaperonins help folding the polypeptide chain(know about hydrogen bonds but mechanism...)? like enzyme?What's their origin? And did "first cell" contain genes for them?What if there would be a mutation and and some chaperonin would be nonfunctional? Would it be lethal?
How do polypeptide chains form protein with quaternary structure(are there also some helpers -exept chap.)?
Maybe sounded stupid but you can easily lost in details   :-[
Thanks in advance!
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Offline constant thinker

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Re:protein folding
« Reply #1 on: May 25, 2005, 04:29:44 PM »
I'd suggest looking at the cells processes. Look it up on google. Howstuffworks.com has a good how cells work. It won't tell you about what your asking but will give some more background.

****Note: Enzymes are catalysts. I messed up. I wasn't thinking clearly because I seamed to have forgetten what a catalyst was for some reason.

Best of luck.
« Last Edit: May 26, 2005, 03:46:18 PM by constant thinker »
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"The nine most terrifying words in the English language are, 'I'm from the government and I'm here to help.' " -Ronald Reagan

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savoy7

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Re:protein folding
« Reply #2 on: May 25, 2005, 11:36:10 PM »
search
chaperone or hsp 60 or 70

heat shock proteins (hsp) were first written about in the early 90's.  They proteins were later called chaperones.  They bonded to hydrophobic regions of "molten" globulin after it was formed from the ribosomes.  Primary and secondary proteins can be made without help of a chaperone, but tertiary forms need help folding.  

Give those words a search and if you want more info I can provide some (I'm not totally up to date on the current research, but I can provide a little insight).


side note: constant thinker - What do you mean "Enzymes break down not build up"
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Offline constant thinker

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Re:protein folding
« Reply #3 on: May 26, 2005, 03:47:06 PM »
I was wrong about what I said about enzymes and have changed it. Sorry it was very stupid of me.
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"The nine most terrifying words in the English language are, 'I'm from the government and I'm here to help.' " -Ronald Reagan

"I'm for anything that gets you through the night, be it prayer, tranquilizers, or a bottle of Jack Daniels." -Frank Sinatra

Zami87

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Re:protein folding
« Reply #4 on: May 31, 2005, 11:57:00 AM »
Hi! Thanks! :)I did little search and I think that I understand mechanism now but still I didn't find answers to most of my questions
What's their origin? And did "first cell" contain genes for them?
What if there would be a mutation and and some chaperonin would be nonfunctional? Would it be lethal?
now I read that ribosomes in prokaryotes don't have chaperonins function so it would be lethal for prokaryotes but I'm not sure for eukaryotes cause their ribosomes have that function ...so does that mean that most of mutations in genes for chaperones wouldn't be lethal?
And I read that mutation for hsp90 would be lethal in early  embrionic stage....
Now do you know some diseases related to non functional chaperones? And if someone has idea about my previous questions, just an idea ??? ..THANKS!!!!
ps most informations from  :)http://www.chaperone.sote.hu/Examples.html
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