Sandbox reserved 457: Difference between revisions
No edit summary |
No edit summary |
||
Line 15: | Line 15: | ||
== Structure == | == Structure == | ||
The secondary structure contains 2 identical amino acid chains with 143 residues per chain. It also contains 14 alpha helices per chain and no beta sheets. Deoxy-leghemoglobin has a proximal histidine. The imidazole rotates between two different positions, forming an eclipsed position. The proximal histidine increases the steric hindrance, while it has a staggered position in oxy-leghemoglobin. These opposite positions between oxy- and deoxy- leghemoglobin allow for a reduced activation energy for the reaction between leghemoglobin and oxygen. <ref>http://www.rcsb.org/pdb/explore/explore.do?structureId=2GDM<ref> | The secondary structure contains 2 identical amino acid chains with 143 residues per chain. It also contains 14 alpha helices per chain and no beta sheets. Deoxy-leghemoglobin has a proximal histidine. The imidazole rotates between two different positions, forming an eclipsed position. The proximal histidine increases the steric hindrance, while it has a staggered position in oxy-leghemoglobin. These opposite positions between oxy- and deoxy- leghemoglobin allow for a reduced activation energy for the reaction between leghemoglobin and oxygen. <ref>http://www.rcsb.org/pdb/explore/explore.do?structureId=2GDM</ref> | ||
== See Also == | == See Also == |