denature

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Ryan Sutcliffe

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Feb 8, 2012, 10:31:11 PM2/8/12
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I know that having the temperature too high or the pH too acidic will
denature an enzyme but i cant find what the third way enzymes can be
denatured

Harkness

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Feb 8, 2012, 10:59:19 PM2/8/12
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...non-competitive inhibitors
A little different mechanism than pH and temp since the inhibitors
only change the shape of the active site and not the whole protein.
This way the protein is still functional once the inhibitor
leaves...unlike denaturing by pH or temp

Joe C

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Feb 9, 2012, 10:30:48 PM2/9/12
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If non-competitive inhibitors change the shape of the active site in
the protein but they are still functional what does a protein do after
that?

Harkness

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Feb 9, 2012, 10:41:54 PM2/9/12
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Once the inhibitor leaves and the active site is back to normal the
enzyme can bind the substrate like it was supposed to

Joe C

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Feb 9, 2012, 10:45:23 PM2/9/12
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If Cofactors change the shape of the active site does it go back to
normal?

Joe C

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Feb 9, 2012, 10:58:38 PM2/9/12
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And is it a good thing when cofactors change the shape of enzymes?
They seem similar to non-competitive inhibitors

Harkness

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Feb 9, 2012, 11:24:26 PM2/9/12
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Yes, shape will go back to normal

Mélanie Girard

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Feb 10, 2012, 12:14:12 AM2/10/12
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Yea... I'm not really understanding the difference between cofactors
and non competitive inhibitors... They both bind to allosteric sites
and cause shape change... So what's the difference?

Harkness

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Feb 10, 2012, 12:21:34 AM2/10/12
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Cofactors are good. They facilitate the enzymatic action where non-
competitive inhibitors prevent enzymes from functioning. Same process.
Opposite outcomes
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