Sandbox 46: Difference between revisions

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This secondary structure is oriented as such so that the <scene name='Sandbox_46/1ake_phobicphilic/2'>hydrophobic and hydrophilic residues</scene> are buried or exposed depending on their individual properties. The hydrophobic, represented in grey, are buried as to avoid as much contact with water as possible. Similarly, the hydrophilic, or polar, residues are colored purple and exposed as much to water as possible. This is further illustrated by the <scene name='Sandbox_46/1ake_water/1'>water solvation</scene> model, displaying water molecules as pink orbs and the enzyme as a translucent white. These hydrophobic interactions, burying of non polar residues and exposure of polar ones, is another main driving force conserving the tertiary structure of the enzyme.

The model of adenylate kinases shows displays the non-hydrolysable substrate as the ligand. The <scene name='Sandbox_46/1ake_ligandinteract/1'>residues interacting with the ligand</scene> are polar as the substrate is also highly negatively charged.

The model of adenylate kinases shows displays the non-hydrolysable substrate as the ligand. The <scene name='Sandbox_46/1ake_ligandinteract/1'>residues interacting with the ligand</scene> are polar as the substrate is also highly negatively charged. The ligand in this model is , as evidenced by the stick structure with the standard atomic color scheme.

Sandbox 46: Difference between revisions

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Revision as of 19:33, 18 October 2012 view source Student (talk \| contribs) students 33,923 edits No edit summary ← Older edit		Revision as of 19:45, 18 October 2012 view source Student (talk \| contribs) students 33,923 edits No edit summary Newer edit →
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	This secondary structure is oriented as such so that the <scene name='Sandbox_46/1ake_phobicphilic/2'>hydrophobic and hydrophilic residues</scene> are buried or exposed depending on their individual properties. The hydrophobic, represented in grey, are buried as to avoid as much contact with water as possible. Similarly, the hydrophilic, or polar, residues are colored purple and exposed as much to water as possible. This is further illustrated by the <scene name='Sandbox_46/1ake_water/1'>water solvation</scene> model, displaying water molecules as pink orbs and the enzyme as a translucent white. These hydrophobic interactions, burying of non polar residues and exposure of polar ones, is another main driving force conserving the tertiary structure of the enzyme.		This secondary structure is oriented as such so that the <scene name='Sandbox_46/1ake_phobicphilic/2'>hydrophobic and hydrophilic residues</scene> are buried or exposed depending on their individual properties. The hydrophobic, represented in grey, are buried as to avoid as much contact with water as possible. Similarly, the hydrophilic, or polar, residues are colored purple and exposed as much to water as possible. This is further illustrated by the <scene name='Sandbox_46/1ake_water/1'>water solvation</scene> model, displaying water molecules as pink orbs and the enzyme as a translucent white. These hydrophobic interactions, burying of non polar residues and exposure of polar ones, is another main driving force conserving the tertiary structure of the enzyme.

	The model of adenylate kinases shows displays the non-hydrolysable substrate as the ligand. The <scene name='Sandbox_46/1ake_ligandinteract/1'>residues interacting with the ligand</scene> are polar as the substrate is also highly negatively charged.		The model of adenylate kinases shows displays the non-hydrolysable substrate as the ligand. The <scene name='Sandbox_46/1ake_ligandinteract/1'>residues interacting with the ligand</scene> are polar as the substrate is also highly negatively charged. The ligand in this model is , as evidenced by the stick structure with the standard atomic color scheme.