Sandbox reserved 457: Difference between revisions
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== 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 == | ||
[[hemoglobin]] | [[hemoglobin]] | ||
[[myoglobin]] | [[myoglobin]] | ||
[[hemeproteins]] | |||
== References == | == References == | ||
<references/> | <references/> | ||