Sandbox Reserved 1798: Difference between revisions
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Here is the MqnA <scene name="/12/3456/Sample/1">color</scene> by Group, and <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Here are the alpha-helices. You can see the substrate buried deep within the enzyme. It is dehydrated by the interaction described above. The dimer is illustrated as two separate colors of the enzyme. The two sides work together in the VFT motion to form the new substrate, EPB. | Here is the MqnA <scene name="/12/3456/Sample/1">color</scene> by Group, and <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. Here are the alpha-helices. You can see the substrate buried deep within the enzyme. It is dehydrated by the interaction described above. The dimer is illustrated as two separate colors of the enzyme. The two sides work together in the VFT motion to form the new substrate, EPB. | ||
Here are the main <scene name='95/954095/Secondary_structure/ | Here are the main <scene name='95/954095/Secondary_structure/6'>secondary structures</scene>, which are, in effect, the residues that do the binding, the ligands. | ||
Here are the main tertiary and quaternary features. Namely, the alpha-helices and the dimer protein, as illustrated by the bi-color cartoon. | Here are the main tertiary and quaternary features. Namely, the alpha-helices and the dimer protein, as illustrated by the bi-color cartoon. | ||
