Myoglobin: Difference between revisions

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<b>Caution</b>: The text in this article and has not been updated to reflect what is actually available on this page. There is <b>no zoom slider</b> and <b>no animate button</b>. These were formerly present when an earlier version of Proteopedia supported Kinemages. A volunteer is needed to clean up and improve this article on a pedagogically and historically important protein. Green links are needed!

~~<font color="gray">Text referring to the now absent Kinemage is in italics.</font>~~

~~[[User:Eric Martz|Eric Martz]] 01:09, 13 September 2014 (IDT)~~

~~</td></tr></table>~~

[[Myoglobin]] is a globular protein whose function is to store molecular oxygen in muscles (myo = muscles). It has two main components: a single polypeptide chain, and heme ligand. The heme ligand is only <scene name='23/238129/Transparent_spacefill/2'>partially exposed</scene> to the surface; the majority of it is buried inside the protein. The overall <scene name='23/238129/Surface/1'>shape</scene> of myoglobin is approximately disc-shaped with a diameter that is about twice its thickness. The overall fold of the protein is conserved, especially the <scene name='23/238129/Hydrophobic/1'>hydrophobic</scene> core of the protein (shown in purple), but the sequence is more <scene name='23/238129/Conserved_cartoon/1'>variable</scene> on the surface. {{Template:~~ColorKey_ConSurf~~}}

[[Myoglobin]] is a globular protein whose function is to store molecular oxygen in muscles (myo = muscles). It has two main components: a single polypeptide chain, and heme ligand. The heme ligand is only <scene name='23/238129/Transparent_spacefill/2'>partially exposed</scene> to the surface; the majority of it is buried inside the protein. The overall <scene name='23/238129/Surface/1'>shape</scene> of myoglobin is approximately disc-shaped with a diameter that is about twice its thickness. The overall fold of the protein is conserved, especially the <scene name='23/238129/Hydrophobic/1'>hydrophobic</scene> core of the protein (shown in purple), but the sequence is more <scene name='23/238129/Conserved_cartoon/1'>variable</scene> on the surface. {{Template:ColorKey_ConSurf_NoYellow_NoGray}}

The globin consists mostly of [[Helices in Proteins|alpha helices]] shown in <scene name='23/238129/2ndary_structure/2'>pink</scene>; it has no beta sheets and its nonhelical segments mostly serve as links that connect the helices. Look down the barrel of some of the longer helices. Are they all straight? The eight structurally conserved alpha helices are labelled <scene name='23/238129/Helix_labels/2'>A through H</scene>. The protein is colored as a N-->C rainbow in this view; the N terminus is blue, while the C terminus is red.

Myoglobin: Difference between revisions

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@@ Line 1: / Line 1: @@
-<table style="background:#ffffa0;" cellpadding="8" border="1"><tr><td>
-<b>Caution</b>: The text in this article and has not been updated to reflect what is actually available on this page. There is <b>no zoom slider</b> and <b>no animate button</b>. These were formerly present when an earlier version of Proteopedia supported Kinemages. A volunteer is needed to clean up and improve this article on a pedagogically and historically important protein. Green links are needed!
-<font color="gray">Text referring to the now absent Kinemage is in italics.</font>
-[[User:Eric Martz|Eric Martz]] 01:09, 13 September 2014 (IDT)
-</td></tr></table>
 <StructureSection load='1a6m' size='350' side='right' caption='Structure of Sperm whale myoglobin with O2 and sulfate (PDB entry [[1a6m]])' scene=''>
-[[Myoglobin]] is a globular protein whose function is to store molecular oxygen in muscles (myo = muscles).  It has two main components:  a single polypeptide chain, and heme ligand.  The heme ligand is only <scene name='23/238129/Transparent_spacefill/2'>partially exposed</scene> to the surface; the majority of it is buried inside the protein. The overall <scene name='23/238129/Surface/1'>shape</scene> of myoglobin is approximately disc-shaped with a diameter that is about twice its thickness.  The overall fold of the protein is conserved, especially the <scene name='23/238129/Hydrophobic/1'>hydrophobic</scene> core of the protein (shown in purple),  but the sequence is more <scene name='23/238129/Conserved_cartoon/1'>variable</scene> on the surface.  {{Template:ColorKey_ConSurf}}
+[[Myoglobin]] is a globular protein whose function is to store molecular oxygen in muscles (myo = muscles).  It has two main components:  a single polypeptide chain, and heme ligand.  The heme ligand is only <scene name='23/238129/Transparent_spacefill/2'>partially exposed</scene> to the surface; the majority of it is buried inside the protein. The overall <scene name='23/238129/Surface/1'>shape</scene> of myoglobin is approximately disc-shaped with a diameter that is about twice its thickness.  The overall fold of the protein is conserved, especially the <scene name='23/238129/Hydrophobic/1'>hydrophobic</scene> core of the protein (shown in purple),  but the sequence is more <scene name='23/238129/Conserved_cartoon/1'>variable</scene> on the surface.  {{Template:ColorKey_ConSurf_NoYellow_NoGray}}
 The globin consists mostly of [[Helices in Proteins|alpha helices]] shown in <scene name='23/238129/2ndary_structure/2'>pink</scene>; it has no beta sheets and its nonhelical segments mostly serve as links that connect the helices. Look down the barrel of some of the longer helices. Are they all straight? The eight structurally conserved alpha helices are labelled <scene name='23/238129/Helix_labels/2'>A through H</scene>.  The protein is colored as a N-->C rainbow in this view; the N terminus is blue, while the C terminus is red.