Trypsin: Difference between revisions

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=Introduction=

Trypsin is a medium size globular protein that functions as a pancreatic serine protease. This enzyme hydrolyzes bonds by cleaving peptides on the C-terminal side of the amino acid residues lysine and arginine. It has also been shown that cleavage will not occur if there is a proline residue on the carboxyl side of the cleavage site. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme. In 1931 the enzyme was purified by crystallization by Norothrop and Kunitz and later in 1974 the three dimensional structure of trypsin was determined. Throughout the 1990's the role of trypsin in hereditary pancreatitis and the mutation that causes it was discovered. Today trypsin is used in the development of cell and tissue protocols, as well as in the medical field to determine the role of trypsin in pancreatic diseases<ref>Trypsin. 2010. 30 October 2010 <http://www.worthington-biochem.com/tyr/default.html></ref>.

Trypsin is a medium size globular protein that functions as a pancreatic serine protease. This enzyme hydrolyzes bonds by cleaving peptides on the C-terminal side of the amino acid residues lysine and arginine. It has also been shown that cleavage will not occur if there is a proline residue on the carboxyl side of the cleavage site. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme. In 1931 the enzyme was purified by crystallization by Norothrop and Kunitz and later in 1974 the three dimensional structure of trypsin was determined.The buffer salts associated with the protein were used to crystallize trypsin. Throughout the 1990's the role of trypsin in hereditary pancreatitis and the mutation that causes it was discovered. Today trypsin is used in the development of cell and tissue protocols, as well as in the medical field to determine the role of trypsin in pancreatic diseases<ref>Trypsin. 2010. 30 October 2010 <http://www.worthington-biochem.com/tyr/default.html></ref>.

[[Image:Tryogen.gif |thumb|left|Trypsinogen]]

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There are three <scene name='Sandbox_32/Disulfide_bonds/1'>disulfide bonds</scene> in the Trypsin protein. These bonds occur between Cysteine residues and are shown in yellow in this image of the protein. The remainder of the protein is shown in grey. Disulfide bonds in a protein act as stabilizing forces that occur within and between polypeptide chains.

~~==Ions and Their Intermolecular Forces Between them and the Protein==~~

The Trypsin protein has <scene name='Sandbox_32/Ions_in_protein/1'>ligands</scene> that interact with other aspects of the protein. These ligands are shown in the figure as the red and yellow compounds, while the remainder of the protein is white in color. Three of the four ligands contain four oxygen atoms (red) and one Sulfur atom (yellow). The final ligand contains two Oxygen atoms and one Sulfur atom. <applet scene='Sandbox_32/Secondary_structure/1' size='350' frame='true' align='true' align='right' caption='Trypsin protein with structural aspects shown.'/>

The interactions between the <scene name='Sandbox_32/Sulfur_ion_interactions/1'>Sulfur atoms</scene> are shown in this figure. The Sulfur atoms are shown in green and the ball and stick model shows the parts of the protein that are interacting with the corresponding Sulfur atoms. The remaining parts of the protein interacting with the green Sulfur atoms are the certain parts of the nearby amino acid residues. The Sulfur atoms shown in white in this figure can be ignored since they are related to the Sulfur atoms in the disulfide bonds.

The interactions between the <scene name='Sandbox_32/Oxygen_ion_interactions/2'>Oxygen atoms</scene> are shown in this figure. The Oxygen atoms are shown in red and the ball and stick model shows the parts of the protein that are interacting with the corresponding Oxygen atoms.

The composition of the Trypsin protein can be seen when surrounded <scene name='Sandbox_32/Compostion/2'>water molecules</scene>. This image shows where and how water molecules bond to the protein. The water molecules are blue, while the protein is an off-white color. These interactions are important when it comes to how the protein interacts with its environment.

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@@ Line 1: / Line 1: @@
 =Introduction=
-Trypsin is a medium size globular protein that functions as a pancreatic serine protease. This enzyme hydrolyzes bonds by cleaving peptides on the C-terminal side of the amino acid residues lysine and arginine. It has also been shown that cleavage will not occur if there is a proline residue on the carboxyl side of the cleavage site. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme. In 1931 the enzyme was purified by crystallization by Norothrop and Kunitz and later in 1974 the three dimensional structure of trypsin was determined. Throughout the 1990's the role of trypsin in hereditary pancreatitis and the mutation that causes it was discovered.  Today trypsin is used in the development of cell and tissue protocols, as well as in the medical field to determine the role of trypsin in pancreatic diseases<ref>Trypsin. 2010. 30 October 2010 <http://www.worthington-biochem.com/tyr/default.html></ref>.
+Trypsin is a medium size globular protein that functions as a pancreatic serine protease. This enzyme hydrolyzes bonds by cleaving peptides on the C-terminal side of the amino acid residues lysine and arginine. It has also been shown that cleavage will not occur if there is a proline residue on the carboxyl side of the cleavage site. Trypsin was first discovered in 1876 by Kuhne, who investigated the proteolytic activity of the enzyme. In 1931 the enzyme was purified by crystallization by Norothrop and Kunitz and later in 1974 the three dimensional structure of trypsin was determined.The buffer salts associated with the protein were used to crystallize trypsin. Throughout the 1990's the role of trypsin in hereditary pancreatitis and the mutation that causes it was discovered.  Today trypsin is used in the development of cell and tissue protocols, as well as in the medical field to determine the role of trypsin in pancreatic diseases<ref>Trypsin. 2010. 30 October 2010 <http://www.worthington-biochem.com/tyr/default.html></ref>.
 [[Image:Tryogen.gif |thumb|left|Trypsinogen]]
@@ Line 19: / Line 20: @@
 There are three <scene name='Sandbox_32/Disulfide_bonds/1'>disulfide bonds</scene> in the Trypsin protein. These bonds occur between Cysteine residues and are shown in yellow in this image of the protein. The remainder of the protein is shown in grey. Disulfide bonds in a protein act as stabilizing forces that occur within and between polypeptide chains.
-==Ions and Their Intermolecular Forces Between them and the Protein==
-The Trypsin protein has <scene name='Sandbox_32/Ions_in_protein/1'>ligands</scene> that interact with other aspects of the protein. These ligands are shown in the figure as the red and yellow compounds, while the remainder of the protein is white in color. Three of the four ligands contain four oxygen atoms (red) and one Sulfur atom (yellow). The final ligand contains two Oxygen atoms and one Sulfur atom. <applet scene='Sandbox_32/Secondary_structure/1' size='350' frame='true' align='true' align='right' caption='Trypsin protein with structural aspects shown.'/>
-The interactions between the <scene name='Sandbox_32/Sulfur_ion_interactions/1'>Sulfur atoms</scene> are shown in this figure. The Sulfur atoms are shown in green and the ball and stick model shows the parts of the protein that are interacting with the corresponding Sulfur atoms. The remaining parts of the protein interacting with the green Sulfur atoms are the certain parts of the nearby amino acid residues. The Sulfur atoms shown in white in this figure can be ignored since they are related to the Sulfur atoms in the disulfide bonds.
-The interactions between the <scene name='Sandbox_32/Oxygen_ion_interactions/2'>Oxygen atoms</scene> are shown in this figure. The Oxygen atoms are shown in red and the ball and stick model shows the parts of the protein that are interacting with the corresponding Oxygen atoms.
 The composition of the Trypsin protein can be seen when surrounded <scene name='Sandbox_32/Compostion/2'>water molecules</scene>. This image shows where and how water molecules bond to the protein. The water molecules are blue, while the protein is an off-white color. These interactions are important when it comes to how the protein interacts with its environment.