Sandbox 50: Difference between revisions
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Trypsin's distribution of <scene name='Sandbox_50/Nonpolarandpolar/1'>polar and nonpolar residues</scene> follow the rules of the hydrophobic effect. The nonpolar (gray) residues are located on the interior of the protein so they can be shielded from water, while the polar (purple) residues are distributed on the exterior of the protein because they can interact with water. This <scene name='Sandbox_50/Nonpolarandpolarspacefilled/1'>spacefill</scene> model shows the distribution of the hydrophilic and hydrophobic residues and the actual space they occupy. Again the hydrophobic, nonpolar residues are shown in gray, and the hydrophilic, polar residues are purple. This type of residue distribution in trypsin is entropically favorable becuase the water surrounding the protein does not become ordered. | Trypsin's distribution of <scene name='Sandbox_50/Nonpolarandpolar/1'>polar and nonpolar residues</scene> follow the rules of the hydrophobic effect. The nonpolar (gray) residues are located on the interior of the protein so they can be shielded from water, while the polar (purple) residues are distributed on the exterior of the protein because they can interact with water. This <scene name='Sandbox_50/Nonpolarandpolarspacefilled/1'>spacefill</scene> model shows the distribution of the hydrophilic and hydrophobic residues and the actual space they occupy. Again the hydrophobic, nonpolar residues are shown in gray, and the hydrophilic, polar residues are purple. This type of residue distribution in trypsin is entropically favorable becuase the water surrounding the protein does not become ordered. | ||
==Attractions Between Structural Components and the Remainder of the Protein== | ==Attractions Between Structural Components and the Remainder of the Protein== | ||
===Disulfide Bonds=== | |||
Trypsin contains three -disulfide bonds- involving six cysteine residues. These disulfide bonds stabalize the tertiary structure of Trypsin. | |||