Sandbox 44
From Proteopedia
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Observing the '''Rainbow Coloration''' of trypsin one can easily follow the primary sequence of the amino acids as it begins at the amide end with the color blue, and continues and progresses to the carboxyl end with the final 58th amino acid reside colored pink. | Observing the '''Rainbow Coloration''' of trypsin one can easily follow the primary sequence of the amino acids as it begins at the amide end with the color blue, and continues and progresses to the carboxyl end with 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. | + | 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. |
| + | |||
| + | To determine the polar and non-polar sections of an enzyme, the various R groups coming of of the '''protein's backbone''' are analyzed. Looking at the '''R groups''', the side chains can be classified as either non-polar otherwise known as hydrophobic (literally meaning water fearing) or polar otherwise known as hydrophilic (water loving). | ||
==Function== | ==Function== | ||
Revision as of 23:40, 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. |
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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 sequence of the amino acids as it begins at the amide end with the color blue, and continues and progresses to the carboxyl end with 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.
To determine the polar and non-polar sections of an enzyme, the various R groups coming of of the protein's backbone are analyzed. Looking at the R groups, the side chains can be classified as either non-polar otherwise known as hydrophobic (literally meaning water fearing) or polar otherwise known as hydrophilic (water loving).
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.)
