Sandbox 39: Difference between revisions
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== Polarity and Hydrophobicity == | == Polarity and Hydrophobicity == | ||
Papain contains many hydrophobic, or "water-hating" regions, and hydrophillic, or "water-loving" regions. The hydrophobic effect, or the tendency of nonpolar substances to aggregate in aqueous solution and exclude water molecules, allows proteins to fold the way they do, exposing hydrophilic residues on their outer surface while sequestering hydrophobic residues in their center. As shown above, all of the <scene name='Sandbox_39/ | Papain contains many hydrophobic, or "water-hating" regions, and hydrophillic, or "water-loving" regions. The hydrophobic effect, or the tendency of nonpolar substances to aggregate in aqueous solution and exclude water molecules, allows proteins to fold the way they do, exposing hydrophilic residues on their outer surface while sequestering hydrophobic residues in their center. As shown above, all of the <scene name='Sandbox_39/Hydrophobic_residues_revised/1'>hydrophobic residues</scene> are found closer to the center of the folded protein, shown at the left in pink, while the <scene name='Sandbox_39/Hydrophillic_residues_revised/1'>hydrophilic residues</scene> are found around the outside of the protein, shown in blue. These spacefill models give a better idea of the surface area of the protein that contacts the aqueous solution. | ||
== Disulfide Bonds == | == Disulfide Bonds == | ||
