Sandbox 50: Difference between revisions

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Trypsin contains three <scene name='Sandbox_50/Disulfidebonds/1'>disulfide bonds</scene> involving six cysteine residues. These disulfide bonds are intramolecular forces that stabalize the tertiary structure of Trypsin. The figure shows the yellow disulfide bonds between the cysteine residues connecting two random coils, connecting one of the alpha helices to the beta sheet, and the other disulfide connecting the two alpha helices.

===Residue Charge===

This -charge figure- shows the different charges of the amino acid residues that make up Trypsin. The blue residues have cationic side chains, the red residues have anionic side chains, the light purple are the polar, uncharged residues, and the gray residues are hydrophobic. When compared to the spacefilled figure above, the direct correlation between polarity of the side chain and charge of the side chain can be seen. Those residues with charged (blue and red) side chains as well as the polar, uncharged residues are the residues on the exterior of the protein, while the hydrophobic residues remain at the protein's core. Those residues that are cationic and anionic are able to participate in salt bridges.

This <scene name='Sandbox_50/Charged/1'>charge figure</scene> shows the different charges of the amino acid residues that make up Trypsin. The blue residues have cationic side chains, the red residues have anionic side chains, the light purple are the polar, uncharged residues, and the gray residues are hydrophobic. When compared to the spacefilled figure above, the direct correlation between polarity of the side chain and charge of the side chain can be seen. Those residues with charged (blue and red) side chains as well as the polar, uncharged residues are the residues on the exterior of the protein, while the hydrophobic residues remain at the protein's core. Those residues that are cationic and anionic are able to participate in salt bridges.

==Ligand Contacts==

Sandbox 50: Difference between revisions

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@@ Line 13: / Line 13: @@
 Trypsin contains three <scene name='Sandbox_50/Disulfidebonds/1'>disulfide bonds</scene> involving six cysteine residues. These disulfide bonds are intramolecular forces that stabalize the tertiary structure of Trypsin. The figure shows the yellow disulfide bonds between the cysteine residues connecting two random coils, connecting one of the alpha helices to the beta sheet, and the other disulfide connecting the two alpha helices.
 ===Residue Charge===
-This -charge figure- shows the different charges of the amino acid residues that make up Trypsin. The blue residues have cationic side chains, the red residues have anionic side chains, the light purple are the polar, uncharged residues, and the gray residues are hydrophobic. When compared to the spacefilled figure above, the direct correlation between polarity of the side chain and charge of the side chain can be seen. Those residues with charged (blue and red) side chains as well as the polar, uncharged residues are the residues on the exterior of the protein, while the hydrophobic residues remain at the protein's core. Those residues that are cationic and anionic are able to participate in salt bridges.
+This <scene name='Sandbox_50/Charged/1'>charge figure</scene> shows the different charges of the amino acid residues that make up Trypsin. The blue residues have cationic side chains, the red residues have anionic side chains, the light purple are the polar, uncharged residues, and the gray residues are hydrophobic. When compared to the spacefilled figure above, the direct correlation between polarity of the side chain and charge of the side chain can be seen. Those residues with charged (blue and red) side chains as well as the polar, uncharged residues are the residues on the exterior of the protein, while the hydrophobic residues remain at the protein's core. Those residues that are cationic and anionic are able to participate in salt bridges.
 ==Ligand Contacts==