User:Michael Roberts/BIOL115 Myo
From Proteopedia
(Difference between revisions)
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This next view simplifies things, and just shows a <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/9'>cartoon representation </scene>of the secondary structure of the protein. | This next view simplifies things, and just shows a <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/9'>cartoon representation </scene>of the secondary structure of the protein. | ||
| - | You see how the <scene name='User:Michael_Roberts/BIOL115_Myo/Hbonds/1'>hydrogen bonds</scene>that maintain the main secondary structure of the protein are arranged in this next view. | + | You see how the <scene name='User:Michael_Roberts/BIOL115_Myo/Hbonds/1'>hydrogen bonds</scene> that maintain the main secondary structure of the protein are arranged in this next view. |
'''THE GLOBIN FOLD''': | '''THE GLOBIN FOLD''': | ||
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| - | '''PROXIMAL AND DISTAL HISTIDINES''': | + | '''PROXIMAL AND DISTAL HISTIDINES''': The iron atom sits either side of the side chains of two <scene name='User:Michael_Roberts/BIOL115_Myo/Heme/4'>histidine residues</scene>. |
| - | + | ||
| - | The iron atom sits either side of the side chains of two <scene name='User:Michael_Roberts/BIOL115_Myo/Heme/4'>histidine residues</scene>. | + | |
One of these (coloured cyan) is attached to the iron atom, and is known as the ''proximal'' histidine. The other (green) is called the ''distal'' histidine. | One of these (coloured cyan) is attached to the iron atom, and is known as the ''proximal'' histidine. The other (green) is called the ''distal'' histidine. | ||
'''OXYGEN''': | '''OXYGEN''': | ||
| - | The space between the iron and the distal histidine is where the <scene name='User:Michael_Roberts/BIOL115_Myo/Heme/6'>oxygen </scene>binds. | + | The space between the iron and the distal histidine is where the <scene name='User:Michael_Roberts/BIOL115_Myo/Heme/6'>oxygen</scene> (pink) binds. |
</StructureSection> | </StructureSection> | ||
Revision as of 10:30, 15 April 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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