Sandbox Reserved 640: Difference between revisions

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==Structure==
==Structure==


<Structure load='2GDM' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<Structure load='2GDM' size='350' frame='true' align='right' caption='Structure of Leghemoglobin' scene='Insert optional scene name here' />


The 16 kDa polypeptide leghemoglobin consists of two main subunits, the main globin structure and the iron-encompassing heme (protoporphyrin XI) group.  These two subunits form a molecule structurally similar to Myoglobin (Ref 1).  The globin fold portion of the molecule is the standard globin secondary structure, a series of <scene name='Sandbox_Reserved_640/Alpha_helices/1'>8 alpha helices</scene> (Ref 5).  Depending on the species and specific type of Leghemoglobin, the primary amino acid sequence can differ some, but overall it is well conserved.   
The 16 kDa polypeptide leghemoglobin consists of two main subunits, the main globin structure and the iron-encompassing heme (protoporphyrin XI) group.  These two subunits form a molecule structurally similar to Myoglobin (Ref 1).  The globin fold portion of the molecule is the standard globin secondary structure, a series of <scene name='Sandbox_Reserved_640/Alpha_helices/1'>8 alpha helices</scene> (Ref 5).  Depending on the species and specific type of Leghemoglobin, the primary amino acid sequence can differ some, but overall it is well conserved.