User:Michael Roberts/BIOL115 Myo

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<StructureSection load='1mbo' size='500' side='right' caption='Structure of Myoglobin (PDB entry [[1mbo]])' scene='User:Michael_Roberts/BIOL115_Myo/Start/1'>
<StructureSection load='1mbo' size='500' side='right' caption='Structure of Myoglobin (PDB entry [[1mbo]])' scene='User:Michael_Roberts/BIOL115_Myo/Start/1'>
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'''MOLECULAR MODEL:'''
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== 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.
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'''SECONDARY STRUCTURE''':
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'''SECONDARY STRUCTURE''': 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.
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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.
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You see how the <scene name='User:Michael_Roberts/BIOL115_Myo/Hbonds/1'>hydrogen bonds</scene> (yellow) 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> (yellow) that maintain the main secondary structure of the protein are arranged in this next view.
Some amino acids have specific effects on secondary structure. This next view shows the locations of the <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/11'>PROLINE</scene> residues in myoglobin. You can see that they all fall at the end of a stretch of helix. This is bacause their large side chains do not fit within the straight run of α-helix.
Some amino acids have specific effects on secondary structure. This next view shows the locations of the <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/11'>PROLINE</scene> residues in myoglobin. You can see that they all fall at the end of a stretch of helix. This is bacause their large side chains do not fit within the straight run of α-helix.
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'''THE GLOBIN FOLD''':
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'''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 α-helices pack together tightly, and there is very little space in the centre of the protein.
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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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'''HYDROPHOBICITY''':
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'''HYDROPHOBICITY''': Globular folds like this are characterised by a polar, <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/4'>hydrophilic exterior</scene>, which interacts with the aqueous solvent, and a hydrophobic core.
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Globular folds like this are characterised by a polar, <scene name='User:Michael_Roberts/BIOL115_Myo/Secondary_structure/4'>hydrophilic exterior</scene>, which interacts with the aqueous solvent, and a hydrophobic core.
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{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}
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'''THE HEME GROUP''':
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== The Heme Group ==
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Now let's turn our attention to the main function of myoglobin - oxygen binding.
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.
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.

Revision as of 13:12, 22 April 2013

Crystal Structure of myoglobin, 1a6m
Crystal Structure of myoglobin, 1a6m


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.

Structure of Myoglobin (PDB entry 1mbo)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Michael Roberts

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