User:Michael Roberts/BIOL115 Myo
From Proteopedia
(Difference between revisions)
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Click on the ''' 'green links' ''' in the text in the scrollable section below to examine this molecule in more detail. | Click on the ''' 'green links' ''' in the text in the scrollable section below to examine this molecule in more detail. | ||
| - | <StructureSection load='1mbo' size=' | + | <StructureSection load='1mbo' size='600' side='right' caption='Structure of Myoglobin (PDB entry [[1mbo]])' scene='User:Michael_Roberts/BIOL115_Myo/Start/1'> |
== Molecular model: == | == Molecular model: == | ||
The initial view here is a ball-and-stick representation of the molecular structure of myoglobin. | The initial view here is a ball-and-stick representation of the molecular structure of myoglobin. | ||
Revision as of 16:29, 1 May 2013
The heme group and oxygen binding in myoglobin.
Myoglobin is a protein whose function is to store oxygen in muscle tissues. Like heamoglobin, it is red in colour, and it is myoglobin that gives muscle its strong red colour.
Myoglobin was the first globular protein for which the 3-dimensional structure was solved, back in the late 1950s. It gives its name to the 'globin fold', a common alpha domain motif. An alpha domain is a structural region composed entirley of alpha-helix.
Click on the 'green links' in the text in the scrollable section below to examine this molecule in more detail.
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