Sandbox 38: Difference between revisions
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== '''Hydrophobicity and Hydrophilicity''' == | == '''Hydrophobicity and Hydrophilicity''' == | ||
These charged residues contribute to the overall hydrophobicity (water hating) and hydrophilicity (water loving) portions of the enzyme, as the <scene name='Sandbox_38/Hydrophobic_and_polar_residues/2'>hydrophobic and hydrophilic regions</scene> are a huge factor in determining protein folding. The polar amino acids are indicated by a purple color, while the hydrophobic residues are gray. <scene name='Sandbox_38/Papain_ligand_binding/1'>ligands of Papain</scene> | These charged residues contribute to the overall hydrophobicity (water hating) and hydrophilicity (water loving) portions of the enzyme, as the <scene name='Sandbox_38/Hydrophobic_and_polar_residues/2'>hydrophobic and hydrophilic regions</scene> are a huge factor in determining protein folding. As mentioned before, the charged, hydrophilic, portions of the enzyme are primarily located on the out portion of the molecule. The polar amino acids are indicated by a purple color, while the hydrophobic residues are gray. <scene name='Sandbox_38/Papain_ligand_binding/1'>ligands of Papain</scene> | ||
<scene name='Sandbox_38/Hydrophobic_residues/1'>Hydrophobic Residues</scene>. | <scene name='Sandbox_38/Hydrophobic_residues/1'>Hydrophobic Residues</scene>. | ||
</StructureSection> | </StructureSection> | ||
