User:Michael Roberts/BIOL115 Myo: 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/ | 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. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 17:16, 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.
MOLECULAR MODEL: The initial view here is a ball-and-stick representation of the molecular structure of myoglobin.
SECONDARY STRUCTURE: This next view simplifies things, and just shows a of the secondary structure of the protein. THE GLOBIN FOLD: In this next view, the eight 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.
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