User:Michael Roberts/BIOL115 CaM: Difference between revisions
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The structure on the right, obtained by X-ray crystallography, represents the Ca2+-binding protein calmodulin. It has a dumbell-shaped structure with two identical lobes connected by a central alpha-helix. Each lobe comprises three a helices joined by loops. A helix-loop-helix motif forms the basis of each EF hand. | The structure on the right, obtained by X-ray crystallography, represents the Ca2+-binding protein calmodulin. It has a dumbell-shaped structure with two identical lobes connected by a central alpha-helix. Each lobe comprises three a helices joined by loops. A helix-loop-helix motif forms the basis of each EF hand. | ||
Click on the 'green links' in the text in the scrollable section below to examine this molecule in more detail.<StructureSection load='1cll' size='500' side='right' caption='Structure of Human calmodulin (PDB entry [[1cll]])' scene=''>Anything in this section will appear adjacent to the 3D structure and will be scrollable.</StructureSection> | |||
Let us color the two main forms of regular <scene name='Sandbox_LUBIOL115/Structure_plus_ca/1'>secondary structure</scene> in this protein. Alpha helix appears in red, beta sheet in yellow. | Let us color the two main forms of regular <scene name='Sandbox_LUBIOL115/Structure_plus_ca/1'>secondary structure</scene> in this protein. Alpha helix appears in red, beta sheet in yellow. | ||
