User:Michael Roberts/Open-Day Demo: Difference between revisions
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'''Secondary Structure''' | '''Secondary Structure''' | ||
The <scene name='57/575866/Secondary_sequence/1'>secondary structure</scene> is the local structure over short distances. This level of structure is stabilized by <scene name='57/575866/H_bond_a_helix/1'>hydrogen bonds</scene> along the amino acid backbone. There are only two main forms of secondary structure seen in proteins: alpha helix, which forms coiled cylinders of amino acids, as shown here, and beta | The <scene name='57/575866/Secondary_sequence/1'>secondary structure</scene> is the local structure over short distances. This level of structure is stabilized by <scene name='57/575866/H_bond_a_helix/1'>hydrogen bonds</scene> along the amino acid backbone. There are only two main forms of secondary structure seen in proteins: alpha helix, which forms coiled cylinders of amino acids, as shown here, and beta strands, a planar (flat) arrangement of amino acids which often line up together to from so-called beta sheets. | ||
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== Secondary Structure in chymotrypsin == | |||
Now that we know something about the structural organisation of proteins, let's go back to our chymotrypsin molecule and have another look. This time, we'll display a <scene name='User:Michael_Roberts/BIOL115_Chymo/2ndry_structure/1'>cartoon representation</scene> indicating the main secondary structural elements. We can see that the main structural form in chymotrypsin is the beta strand, (orange), arranged as anti-parallel sheets which form a circular structure known as a beta barrel. You can rotate the molecule so that you can see down through each of the two beta barrels in turn. | |||
''Colour key:'' | |||
{{Template:ColorKey_Helix}}, | |||
{{Template:ColorKey_Strand}}. | |||
</StructureSection> | </StructureSection> |