Sandbox10: Difference between revisions

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The portion of the protein that is shown is the motor domain of the heavy chain. This protein is largely composed of <scene name='Sandbox10/Helix/1'>alpha-helices</scene> connected by randomly oriented chains. There are also several areas of <scene name='Sandbox10/Betasheets/1'>beta-sheets</scene>, both parallel and anti-parallel.

~~<scene name='Sandbox10/Polarnonpolar/1'>yes</scene>,~~

This view shows the <scene name='Sandbox10/Newscene/2'>active sites</scene> of the protein with the ATP analog ADP-Metavanadate bound to one active site and the allosteric inhibitor pentabromopseudilin.

Myosin contains many <scene name='Sandbox10/Polar/1'>polar</scene> side chains on the surface of the protein, but there are also a large number of nonpolar molecules on the surface. The following <scene name='Sandbox10/Hydrophobic/1'>scene</scene> shows a contrast between hydrophobic (gray) and hydrophilic molecules on the surface of the protein.

Myosin contains many <scene name='Sandbox10/Polar/1'>polar</scene> side chains on the surface of the protein, but there are also a large number of nonpolar molecules on the surface. The following <scene name='Sandbox10/Hydrophobic/1'>scene</scene> shows a contrast between hydrophobic (gray) and hydrophilic molecules on the surface of the protein in a <scene name='Sandbox10/Hydrophobic/1'>space-filling view</scene> and a <scene name='Sandbox10/Polarnonpolar/1'>cartoon view</scene>. By looking at these scenes one can see that although hyrbrophobic molecules penetrate the surface of the molecule, there are no areas of high hydrophobic concentration.

Thanks to Fedorov, R., Boehl, M., Tsiavaliaris, G., Hartmann, F.K., Baruch, P., Brenner, B., Martin, R., Knoelker, H.J., Gutzeit, H.O., Manstein, D.J. for their work in resolving the structure of this protein.

Sandbox10: Difference between revisions

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@@ Line 10: / Line 10: @@
 The portion of the protein that is shown is the motor domain of the heavy chain. This protein is largely composed of <scene name='Sandbox10/Helix/1'>alpha-helices</scene> connected by randomly oriented chains. There are also several areas of <scene name='Sandbox10/Betasheets/1'>beta-sheets</scene>, both parallel and anti-parallel.
-<scene name='Sandbox10/Polarnonpolar/1'>yes</scene>,
 This view shows the <scene name='Sandbox10/Newscene/2'>active sites</scene> of the protein with the ATP analog ADP-Metavanadate bound to one active site and the allosteric inhibitor pentabromopseudilin.
-Myosin contains many <scene name='Sandbox10/Polar/1'>polar</scene> side chains on the surface of the protein, but there are also a large number of nonpolar molecules on the surface. The following <scene name='Sandbox10/Hydrophobic/1'>scene</scene> shows a contrast between hydrophobic (gray) and hydrophilic molecules on the surface of the protein.
+Myosin contains many <scene name='Sandbox10/Polar/1'>polar</scene> side chains on the surface of the protein, but there are also a large number of nonpolar molecules on the surface. The following <scene name='Sandbox10/Hydrophobic/1'>scene</scene> shows a contrast between hydrophobic (gray) and hydrophilic molecules on the surface of the protein in a <scene name='Sandbox10/Hydrophobic/1'>space-filling view</scene> and a <scene name='Sandbox10/Polarnonpolar/1'>cartoon view</scene>. By looking at these scenes one can see that although hyrbrophobic molecules penetrate the surface of the molecule, there are no areas of high hydrophobic concentration.
 Thanks to Fedorov, R.,  Boehl, M.,  Tsiavaliaris, G.,  Hartmann, F.K.,  Baruch, P.,  Brenner, B.,  Martin, R.,  Knoelker, H.J.,  Gutzeit, H.O.,  Manstein, D.J. for their work in resolving the structure of this protein.
 {{STRUCTURE_2jhr |  PDB=2jhr  |  SCENE=  }}