rhodopsin.html

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<!-- Page Title: Rhodopsin -->
<h2>Introduction</h2>
<p>
    This script shows the structure of bacteriorhodopsin. Bacteriorhodopsin is a
    typical alpha helical membrane protein. The amphipathic helices in
    bacteriorhodopsin are also compared to those in a typical water soluble
    protein. (Based on 1brd.pdb, Henderson et al. (1990) J.Mol.Biol.
    <strong>213</strong>: 899-929 and 1aep.pdb, Breiter et al. (1991)
    Biochemistry <strong>30</strong>: 603-608)
</p>
<br>

<h2>Rhodopsin 1</h2>
<p>
    This is bacteriorhodopsin from Halobacterium halobium. It is a transmembrane
    protein containing seven alpha helices.
</p>
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<br>

<h2>Rhodopsin 2</h2>
<p>
    Bacteriorhodopsin contains amphipathic helices in which the
    <span style="color:lime;">hydrophobic sidechains</span> point outward so
    they can interact with the fatty acyl chains of the membrane lipids.
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<br>

<h2>Rhodopsin 3</h2>
<p>
    The hydrophilic sidechains (<span style="color:gold;">YELLOW</span>) point
    toward the interior of the protein.
</p>
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<br>

<h2>Rhodopsin 4</h2>
<p>
    Here is a water-soluble protein with five alpha helices.
</p>
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<br>

<h2>Rhodopsin 5</h2>
<p>
    In this case the <span style="color:lime;"> hydrophobic sidechains</span>
    point to the interior of the protein.
</p>
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<h2>Rhodopsin 6</h2>
<p>
    The hydrophilic residues (<span style="color:gold;">YELLOW</span>) point
    outward toward the solvent.
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