User:Michael Roberts/BIOL115 Myo
From Proteopedia
(Difference between revisions)
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'''THE GLOBIN FOLD''': | '''THE GLOBIN FOLD''': | ||
| - | In this next view, the eight <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/3'>individual alpha-helices </scene>are each coloured differently. This gives you an impression of the classic globion fold. The helices pack together tightly, and there is very little space in the centre of the protein. | + | In this next view, the eight <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/3'>individual alpha-helices </scene>are each coloured differently. This gives you an impression of the classic globion fold. The α-helices pack together tightly, and there is very little space in the centre of the protein. |
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| + | '''THE HEME GROUP''': | ||
| + | Now let's turn our attention to the main function of myoglobin - oxygen binding. | ||
| + | Oxygen is bound by a <scene name='User:Michael_Roberts/BIOL115_Myo/Heme/1'>heme group</scene>, which sits in a hydrophobic pocket in the myoglobin protein. | ||
| + | Central to the heme group is an <scene name='User:Michael_Roberts/BIOL115_Myo/Heme/3'>iron (Fe) atom</scene>. | ||
| + | |||
| + | '''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>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 15:44, 12 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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