Sandbox 44
From Proteopedia
| Line 5: | Line 5: | ||
Trypsin is a serine protease that is produced in the pancreas. Serine protease means that it is an enzyme that cleaves amino acid sequences and that a serine is located in the active site of the enzyme. In order to prevent it from breaking down the proteins in the pancreas of the organism that produces it, it is first produced as the inactive zymogen, proenzyme trypsinogen. | Trypsin is a serine protease that is produced in the pancreas. Serine protease means that it is an enzyme that cleaves amino acid sequences and that a serine is located in the active site of the enzyme. In order to prevent it from breaking down the proteins in the pancreas of the organism that produces it, it is first produced as the inactive zymogen, proenzyme trypsinogen. | ||
==Structural Aspects== | ==Structural Aspects== | ||
| - | Trypsin is an enzyme that is composed of one, sequence unique, chain consisting of 58 amino acid residues. Looking at the '''Secondary Structure'''of trypsin one can see it is composed of two alpha helices (in yellow) and two beta sheets (in pink). | + | Trypsin is an enzyme that is composed of one, sequence unique, chain consisting of 58 amino acid residues. Looking at the '''Secondary Structure''' of trypsin one can see it is composed of two alpha helices (in yellow) and two beta sheets (in pink). |
| - | Trypsin is also held together by three '''Di-Sulfide Bonds''' located between the 5 and 55, 14 and 38, and 30 and 51 Cystine | + | Observing the '''Rainbow Coloration''' of trypsin one can easily follow the primary sequnce of the amino acids as it begins amide end with the color blue, and continues and progresses to the final 58th amino acid reside colored pink. |
| + | Trypsin is also held together by three '''Di-Sulfide Bonds''' located between the 5 and 55, 14 and 38, and 30 and 51 Cystine residues. | ||
==Function== | ==Function== | ||
| + | |||
| + | |||
| + | |||
Here is shown the hydrophobic vs hydrophilic <scene name='Sandbox_44/Hydrophilic_vs_polar_residues/2'>structure</scene> of the protein. Polar molecules appear yellow, while nonpolar appear light purple. | Here is shown the hydrophobic vs hydrophilic <scene name='Sandbox_44/Hydrophilic_vs_polar_residues/2'>structure</scene> of the protein. Polar molecules appear yellow, while nonpolar appear light purple. | ||
This is the <scene name='Sandbox_44/Secondary_structure_of_trypsin/1'>Secondary</scene> Structure of trypsin is displayed.(The pink-alpha helix, and the yellow-beta sheets.) | This is the <scene name='Sandbox_44/Secondary_structure_of_trypsin/1'>Secondary</scene> Structure of trypsin is displayed.(The pink-alpha helix, and the yellow-beta sheets.) | ||
Revision as of 23:28, 27 October 2010
| Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013. |
|
Trypsin
Trypsin is a serine protease that is produced in the pancreas. Serine protease means that it is an enzyme that cleaves amino acid sequences and that a serine is located in the active site of the enzyme. In order to prevent it from breaking down the proteins in the pancreas of the organism that produces it, it is first produced as the inactive zymogen, proenzyme trypsinogen.
Structural Aspects
Trypsin is an enzyme that is composed of one, sequence unique, chain consisting of 58 amino acid residues. Looking at the Secondary Structure of trypsin one can see it is composed of two alpha helices (in yellow) and two beta sheets (in pink). Observing the Rainbow Coloration of trypsin one can easily follow the primary sequnce of the amino acids as it begins amide end with the color blue, and continues and progresses to the final 58th amino acid reside colored pink. Trypsin is also held together by three Di-Sulfide Bonds located between the 5 and 55, 14 and 38, and 30 and 51 Cystine residues.
Function
Here is shown the hydrophobic vs hydrophilic of the protein. Polar molecules appear yellow, while nonpolar appear light purple.
This is the Structure of trypsin is displayed.(The pink-alpha helix, and the yellow-beta sheets.)
