Sandbox 38: Difference between revisions
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== '''Composition of Papain''' == | == '''Composition of Papain''' == | ||
There are three <scene name='Sandbox_38/Disulfide_bonds/1'>disulfide bonds</scene> that contribute to the structure of Papain. These bonds are indicated by their yellow color, as they link particular cysteine residues. Throughout this enzyme, there are specific charged residues, indicating the most polar portions of the molecule. These <scene name='Sandbox_38/Charge/3'>charged residues</scene> can be visualized, as the cationic residues are blue in color, while the anionic residues are red. Partially charged residues are simply lighter in color. It is interesting to note that nearly all of these charged residues are located on the outer portion of the molecule in order to interact with the surrounding environment. These charged residues contribute to the overall hydrophobicity and hydrophilicity of the enzyme, as the <scene name='Sandbox_38/Hydrophobic_and_polar_residues/2'>hydrophobic and hydrophilic regions</scene> are also able to be viewed. The polar amino acids have a purple color and 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>. | |||
</StructureSection> | |||
