Sandbox 46: Difference between revisions
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Many factors contribute to protein stabilization. Disulphide bonds form between the Sulfur atoms of two Cysteine residues and assist in the formation of the tertiary structure. This particular form of trypsin contains three <scene name='Sandbox_46/Disulfide_bonds/3'>disulphide bonds</scene> (yellow). These bonds interact between Cysteine residues at positions 5 and 55, 14 and 38, 30 and 51. Disulphide bond two (residues 14 and 38) interacts with two chiral centers; thus, one Sulfur atom interacts with two Sulfur atoms opposite it. Click <scene name='Sandbox_46/Disulfide_bonds_123/1'>here</scene> to see the labeled disulphide bonds. | Many factors contribute to protein stabilization. Disulphide bonds form between the Sulfur atoms of two Cysteine residues and assist in the formation of the tertiary structure. This particular form of trypsin contains three <scene name='Sandbox_46/Disulfide_bonds/3'>disulphide bonds</scene> (yellow). These bonds interact between Cysteine residues at positions 5 and 55, 14 and 38, 30 and 51. Disulphide bond two (residues 14 and 38) interacts with two chiral centers; thus, one Sulfur atom interacts with two Sulfur atoms opposite it. Click <scene name='Sandbox_46/Disulfide_bonds_123/1'>here</scene> to see the labeled disulphide bonds. | ||
In addition to disulphide bonds, Hydrogen bonding plays a large role in stability. As this <scene name='Sandbox_46/Hbonds_backbone/1'>model</scene> suggests, hydrogen bonds are most prominent in alpha helices and beta sheets of the backbone. In alpha helices, hydrogen bonds form between an H-N and a C-O 4 residue away; complementing the specific turn length (3.6 residues). | In addition to disulphide bonds, Hydrogen bonding plays a large role in stability. As this <scene name='Sandbox_46/Hbonds_backbone/1'>model</scene> suggests, hydrogen bonds (orange) are most prominent in alpha helices and beta sheets of the backbone. In alpha helices, hydrogen bonds form between an H-N and a C-O 4 residue away; complementing the specific turn length (3.6 residues). Hydrogen bonds between the <scene name='Sandbox_46/H_bonds_r_groups/1'>sidechain residues</scene> (R groups) provide further stability for the trypsin moiety. | ||
<scene name='Sandbox_46/ | The yellow and red molecules represent <scene name='Sandbox_46/So4/1'>SO4 (2-) molecules</scene> which are not part of the traditional trypsin structure; they were added during crystallization to freeze Trypsin in a specific conformation. Each SO4 molecule is bound to an active site (ball and stick display) in order to prevent interaction with another substrate. Active site inhibition is a prominent method for studying enzymes. | ||
==Function== | ==Function== | ||
