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Chemical Bonds: Extending predictions to larger molecules.
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<font face="Verdana, Arial, Helvetica, sans-serif" size="5" color="#FFFFFF"><strong>Chemical Bonds:</strong> Extending predictions to larger molecules.</font>
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<td><font face="Verdana, Arial, Helvetica, sans-serif" size="4">Polarity of single bonds within larger molecules can make the entire molecule polar or non-polar. By studying how pairs of atoms bond together it can help you to design more complex molecules with specific properties.</font></td>
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<font size="4" face="Verdana, Arial, Helvetica, sans-serif">Below
are two molecules. The one on the left is made by bonding carbon to
carbon (C-C) and carbon to hydrogen (C-H). The electronegativity
difference in both of these bonding pairs (C - C = 0 and
C - H = 0.45) falls into the non-polar range. Because all the bonds
in pentane are non-polar, pentane is non-polar. The only difference
in </font>
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<font size="4" face="Verdana, Arial, Helvetica, sans-serif">1-pentanol
is that an oxygen is added. However, this causes two new bonding
pairs: oxygen-carbon and oxygen-hydrogen. The electronegativity
difference here causes the bonds to be polar (O - C = 0.89 and
O - H = 1.34), so the molecule is considered to be polar. </font>
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<font size="4" face="Verdana, Arial, Helvetica, sans-serif">The
proteins in your body are made by linking up 20 different kinds
amino acids to form very large molecules. Some proteins end up stuck
in the cell membranes. Those proteins typically have a polar section
which interacts with the water inside and outside of the cell, as
well as a non-polar section </font>
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<img width="228" src="glutamine.gif" height="170">
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<td width="35%" align="left">
<img width="250" src="phenylalanine.gif" height="170">
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<font size="4" face="Verdana, Arial, Helvetica, sans-serif">which spans
the actual cell membrane. Above are two of the 20 types of amino acids,
the main difference being in their sidechains which give the amino acids
their properties. Use the electronegativity table above to determine if
the sidechains are polar or non-polar. In other words, </font><strong><font size="4" color="#000000" face="Verdana, Arial, Helvetica, sans-serif">are
there any polar bonds in the sidechains or are all of the bonds non-polar?</font><font size="4" color="#990000" face="Verdana, Arial, Helvetica, sans-serif">
Right-click (or control-click) on the amino acids and use the annotation
tools to highlight any polar bonds you find in the sidechains. Describe
why you picked those bonds to be polar or non-polar in the text area below
the image. </font></strong>
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<strong><font size="4" face="Arial, Helvetica, sans-serif">Which amino
acid would be good to use in the part of the protein that spans the cell
membrane?</font></strong><font size="4" face="Arial, Helvetica, sans-serif">
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glutamine
phenylalanine
either would work well
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<strong><font size="4" face="Arial, Helvetica, sans-serif">Explain why you
made that choice.</font></strong><font size="4" face="Arial, Helvetica, sans-serif">
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