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Protein Folding: Page 11
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<p class="pagetitle"><strong>Protein Folding:</strong> Protein Function</p>
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<td><p class="mainidea">What does folding have to do with how proteins do their jobs?</p></td>
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<p class="subhead">
Folding Creates Important Sites on Proteins
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In order to perform their functions, proteins interact with one or more
other molecules. The folds of a protein create the site(s) for these
interactions by bringing together amino acids from distant parts of the
protein.
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<p class="firstp">Alcohol dehydrogenase is an enzyme that breaks down alcohol, which is toxic if allowed to build up in large amounts. A small molecule called NAD is required by alcohol dehydrogenase to break down the alcohol molecule. <b>NAD binds to the enzyme in a pocket that is created by folds in the protein. </b></p>
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</p> </td>
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<input name="RadioGroup1" type="radio" class="style1" id="RadioGroup1_0" value="radio" checked="checked" selfscript="selectcomponent 2 false; selectcomponent 3 false" script="script:jmol:1:script jmol-adh-init.spt"> </td>
<td width="753"><b>
Original view</b></td>
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<td><b>
Folds that create binding site<br>
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<td colspan="2"><b>NAD is held by the binding site using some of the same kinds of forces that hold the protein folds in place.</b><span class="firstp"> The pocket fits NAD nearly perfectly, and other molecules do not have the correct shape or charge properties to fit.</span><b><br>
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<input script_selected="script:jmol:1:script jmol-nad-hbonds1.spt" script_deselected="script:jmol:1:select ~all_hbonders; hbonds off" name="checkbox" type="checkbox" id="checkbox"> </td>
<td><b>Hydrogen bonds</b></td>
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<input script_selected="script:jmol:1:script jmol-nad-phobic1.spt" script_deselected="script:jmol:1:select ~all_phobic; hbonds off" name="checkbox" type="checkbox" id="checkbox"> </td>
<td><b>Hydrophobic interactions</b></td>
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<p class="question">
On the right is a different small molecule than NAD. Why wouldn't this
molecule bind to alcohol dehydrogenase in place of NAD? (Choose the BEST
answer below).
</p>
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true
it is not the same as NAD
it is smaller than NAD
it is too large to fit in the NAD site
it's the wrong shape, and will not form attractions with the site
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Can Proteins Take the Heat?
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<p class="firstp">
Life on earth is temperature-dependent. Animals cannot function well
when their body temperatures rise substantially above normal
(in humans, 98.7°F). Very high fevers can even be fatal. An important part of the reason for this has to do
with protein structure.
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<p class="firstp">
Increasing temperature adds thermal (heat) energy to molecules. How does
increasing thermal energy affect proteins?
</p>
<p>
On the left is a model of a small folded protein. Like all proteins, its
folds are held in place by both hydrophobic interactions and polar
attractions such as hydrogen bonds.
</p>
<p>
Use the model to explore the effects of temperature on protein
structure. <b>Click "Run" and observe the stability of the protein
shape. Then gradually raise the temperature by clicking on the red
arrowhead. </b>
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Based on what you saw in the model, what do you suppose would happen to
protein binding sites (like the one for NAD) at high temperatures?
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What would you expect to happen to the function of proteins at very high
temperatures?
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the functions would not be affected
the proteins would not be able to function anymore
the functions would happen faster
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