User:Michael Roberts/BIOL115 CaM: Difference between revisions

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Let's start with a simple <scene name='User:Michael_Roberts/BIOL115_CaM/Wireframe/2'>~~wireframe~~ representation </scene>of the protein. This shows all ~~the bonds between~~ the atoms that make up the protein.

'''MOLECULAR MODEL''':

Let's start with a simple <scene name='User:Michael_Roberts/BIOL115_CaM/Wireframe/3'>ball-and-stick representation </scene>of the protein. This shows all the atoms that make up the protein and the bonds between them.

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The terminal helices are folded down concealing their hydrophobic surfaces and the central chain, which is not a helical along its whole length, is not exposed.

'''CALMODULIN INTERACTS WITH ITS TARGET:'''

The Ca2+-bound form of calmodulin with its exposed hydrophobic surfaces that you have already observed can <scene name='User:Michael_Roberts/BIOL115_CaM/Active_calmodulin/1'>interact with a target protein</scene>. It does this by wrapping around a specific sequence on the target molecule, forcing it to adopt an a-helical structure.

The target molecule here is the calmodulin-regulated enzyme, myosin light chain kinase. Only a short sequence from this protein, the calmodulin binding domain, is shown.

The target molecule here (shown in blue) is the calmodulin-regulated enzyme, myosin light chain kinase. Only a short sequence from this protein, the calmodulin binding domain, is shown.

End of section

</StructureSection>

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 <StructureSection load='1cll' size='600' side='right' caption='Structure of Human calmodulin (PDB entry [[1cll]])' scene=''>
-Let's start with a simple <scene name='User:Michael_Roberts/BIOL115_CaM/Wireframe/2'>wireframe representation </scene>of the protein. This shows all the bonds between the atoms that make up the protein.
+'''MOLECULAR MODEL''':
+Let's start with a simple <scene name='User:Michael_Roberts/BIOL115_CaM/Wireframe/3'>ball-and-stick representation </scene>of the protein. This shows all the atoms that make up the protein and the bonds between them.
@@ Line 48: / Line 49: @@
 The terminal helices are folded down concealing their hydrophobic surfaces and the central chain, which is not a helical along its whole length, is not exposed.
 '''CALMODULIN INTERACTS WITH ITS TARGET:'''
 The Ca2+-bound form of calmodulin with its exposed hydrophobic surfaces that you have already observed can <scene name='User:Michael_Roberts/BIOL115_CaM/Active_calmodulin/1'>interact with a target protein</scene>. It does this by wrapping around a specific sequence on the target molecule, forcing it to adopt an a-helical structure.
-The target molecule here is the calmodulin-regulated enzyme, myosin light chain kinase. Only a short sequence from this protein, the calmodulin binding domain, is shown.
+The target molecule here (shown in blue) is the calmodulin-regulated enzyme, myosin light chain kinase. Only a short sequence from this protein, the calmodulin binding domain, is shown.
 End of section
 </StructureSection>