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/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> | ||