Sandbox10: Difference between revisions

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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 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.

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 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. Certain secondardy structures of the proteins can form in a way that places hydrophobic residues on the surface and hydrophobic residues in the interior. The <scene name='Sandbox10/Amphipathic/1'>alpha helix</scene> and <scene name='Sandbox10/Amphipathic_sheet/1'>beta sheet</scene> highlighted in these scenes shows the alternating pattern between hydrophilic and hydrophobic. The repetition is not perfect, but the majority of the residues are in their favored environment.

<scene name='Sandbox10/Ligand/1'>TextToBeDisplayed</scene>

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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-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 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.
+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 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. Certain secondardy structures of the proteins can form in a way that places hydrophobic residues on the surface and hydrophobic residues in the interior. The <scene name='Sandbox10/Amphipathic/1'>alpha helix</scene> and <scene name='Sandbox10/Amphipathic_sheet/1'>beta sheet</scene> highlighted in these scenes shows the alternating pattern between hydrophilic and hydrophobic. The repetition is not perfect, but the majority of the residues are in their favored environment.
 <scene name='Sandbox10/Ligand/1'>TextToBeDisplayed</scene>
 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.