Sandbox Reserved 780
From Proteopedia
(→<scene name='56/563192/Fumarase_dimer/1'>Fumarase</scene>) |
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A moajority of fumarase's secondary structure is composed of <scene name='56/563192/Fumarase_helix/1'>α-helicies</scene> shown in blue. The longer α-helicies are grouped together and appear to form short coiled coils which compse the mid section of the enzyme's structure. Fumarase contains 3 small sections of <scene name='56/563192/Fumarase_sheet/1'>β-sheets</scene>, each consisting of two strands in anti-parallel allignment connected by a short random coil. | A moajority of fumarase's secondary structure is composed of <scene name='56/563192/Fumarase_helix/1'>α-helicies</scene> shown in blue. The longer α-helicies are grouped together and appear to form short coiled coils which compse the mid section of the enzyme's structure. Fumarase contains 3 small sections of <scene name='56/563192/Fumarase_sheet/1'>β-sheets</scene>, each consisting of two strands in anti-parallel allignment connected by a short random coil. | ||
| - | <scene name='56/563192/Fumarase_hbond/2'>Hydrogen Bonding</scene> | + | <scene name='56/563192/Fumarase_hbond/2'>Hydrogen Bonding</scene> within the structure is shown by the thin black lines. The hydrogen bonding is responsible for the shape of th α-helicies and the bonding between the two strands of the β-sheets. H-bonding is also responsible for the general shape of the random coil sections as well. |
| - | <scene name='56/563192/Fumarase_hydrophilic0trans/1'>hydrophobic residues</scene> | + | The <scene name='56/563192/Fumarase_hydrophilic0trans/1'>hydrophobic residues</scene> of fumarase are shown as wire frame in red. Note that they tend to be located on the interior of the protein and tend to be less solvent accessible due to their lack of polarity. on the other hand, the <scene name='56/563192/Fumarase_realhydrophilic/1'>hydrophilic residues</scene> tend to be located on the outer or solvent accessible edges of the protein as they are either polar or charged and would be stabilized by non-covalent interactions with the solvent. |
| - | <scene name='56/563192/ | + | |
| - | </scene> | + | |
<scene name='56/563192/Fumarase_waterligand/1'>water</scene> | <scene name='56/563192/Fumarase_waterligand/1'>water</scene> | ||
<scene name='56/563192/Fumarase_ligandinteraction/1'>Ligand Binding</scene> | <scene name='56/563192/Fumarase_ligandinteraction/1'>Ligand Binding</scene> | ||
<scene name='56/563192/Fumarase_catalyticsites/1'>active site</scene> | <scene name='56/563192/Fumarase_catalyticsites/1'>active site</scene> | ||
Revision as of 11:19, 18 October 2013
| This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807. |
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This is . Fumarase is an enzyme of the citric acid cycle or Kreb's cycle. The function of fumarase is to stereospecifically convert fumarate into L-malate. This specific image (1FUO) is of Fumarase C from E. Coli. It is a dimer bound with 2 ligands; 2 citrate molecules and 2 malate molecules. The two citrate molecules are the two center and the malate molecules are the outer two ligands shown. The fumarate/L-malate conversion is reversible.
A moajority of fumarase's secondary structure is composed of shown in blue. The longer α-helicies are grouped together and appear to form short coiled coils which compse the mid section of the enzyme's structure. Fumarase contains 3 small sections of , each consisting of two strands in anti-parallel allignment connected by a short random coil. within the structure is shown by the thin black lines. The hydrogen bonding is responsible for the shape of th α-helicies and the bonding between the two strands of the β-sheets. H-bonding is also responsible for the general shape of the random coil sections as well. The of fumarase are shown as wire frame in red. Note that they tend to be located on the interior of the protein and tend to be less solvent accessible due to their lack of polarity. on the other hand, the tend to be located on the outer or solvent accessible edges of the protein as they are either polar or charged and would be stabilized by non-covalent interactions with the solvent.
