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>.

~~=Structure=~~

~~The <scene name='Sandbox_32/N-c_rainbow/2'>pathway</scene> of the protein can be followed from N-terminus of the protein (blue) to the C-terminus of the protein (red).~~

Trypsin has many important structural aspects. The <applet scene='Sandbox_32/Secondary_structure/1' size='350' frame='true' align='true' align='right' caption='Trypsin protein with structural aspects shown.'/>secondary structures are shown this figure <scene name='Sandbox_32/Secondary_structure/1'>(Secondary Structure)</scene>. The ordered non-structured regions of the trypsin protein is shown in yellow <scene name='Sandbox_32/Secondary_structure_main_chain/1'>(ordered non-structured regions)</scene>. Trypsin has two alpha helices shown in blue <scene name='Sandbox_32/Secondary_structure_alpha/1'>(alpha helices)</scene> and two beta sheets shown in green <scene name='Sandbox_32/Secondary_structure_beta/1'>(beta Sheets)</scene>. The beta sheets in the Trypsin protein are antiparallel to each other and connected by a Beta-hairpin turn.

This image shows the <scene name='Sandbox_32/Polar_versus_nonpolar/2'>polarity</scene> of the residues in the protein. The polar areas of the protein are shown in pink, while the non-polar areas of the molecule are shown in light blue. The polarity of the individual amino acid residues can be seen better in the <scene name='Sandbox_32/Polar_vs_non_stick/1'>stick model</scene> or the <scene name='Sandbox_32/Spacefill_polar_vs_nonpolar/2'>spacefill model</scene>. The polar amino acid residues are again shown in pink, while the non-polar amino acid residues are shown in blue. By rotating the three representations of the polar versus non-polar areas of the protein to an aerial view, it can be seen that the polar (hydrophilic) areas are located toward the outside of the protein, while the non-polar (hydrophobic) areas are located toward the inside of the protein.

The charge of the different components of Trypsin are shown in this <scene name='Sandbox_32/Side_chains_charged/1'>charged</scene> figure. The cationic (+) atoms are shown in blue, while the anionic (-) are shown in red. These charged aspects of the protein face the outside environment surrounding the protein. The light purple parts of the protein are uncharged and the gray portions of the protein are hydrophobic. These portions of the protein make up the hydrophobic core of the protein. The charged and uncharged portions of the protein directly relate to the hydrophilic and hydrophobic character of the protein.

The <scene name='Sandbox_32/Side_chains/1'>side chains</scene> are attached to the amino acids residues that make up the protein. In this figure the side chains of the protein are shown in pink and the rest of the protein is shown in grey. There are numerous different side chains represented on the protein. Some of the side chains are aromatic, while others are not. Some side chains are <scene name='Sandbox_32/Side_chains_charged/1'>charged</scene>, while others are uncharged. The type of side chain it is and therefore the corresponding amino acid can be determined by the charge on the side chain.

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.

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.

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

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Trypsin has many applications due to fact that it is easily purified in high quantities. The trypsin enzyme is often used in the research setting to digest proteins and then identify the resulting peptides using mass spectrometry. Trypsin has many uses in the medical field such as dissolving blood clots and treating inflammation. Other applications include its use in pre-digesting of baby food, fingerprinting and sequencing work, and environmental monitoring <ref> Trypsin. 2010. 30 October 2010 <http://www.worthington-biochem.com/tyr/default.html></ref>.

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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>.
-=Structure=
-The <scene name='Sandbox_32/N-c_rainbow/2'>pathway</scene> of the protein can be followed from  N-terminus of the protein (blue) to the C-terminus of the protein (red).
-Trypsin has many important structural aspects. The <applet scene='Sandbox_32/Secondary_structure/1' size='350' frame='true' align='true' align='right' caption='Trypsin protein with structural aspects shown.'/>secondary structures are shown this figure <scene name='Sandbox_32/Secondary_structure/1'>(Secondary Structure)</scene>. The ordered non-structured regions of the trypsin protein is shown in yellow <scene name='Sandbox_32/Secondary_structure_main_chain/1'>(ordered non-structured regions)</scene>. Trypsin has two alpha helices shown in blue <scene name='Sandbox_32/Secondary_structure_alpha/1'>(alpha helices)</scene> and two beta sheets shown in green <scene name='Sandbox_32/Secondary_structure_beta/1'>(beta Sheets)</scene>. The beta sheets in the Trypsin protein are antiparallel to each other and connected by a Beta-hairpin turn.
-This image shows the <scene name='Sandbox_32/Polar_versus_nonpolar/2'>polarity</scene> of the residues in the protein. The polar areas of the protein are shown in pink, while the non-polar areas of the molecule are shown in light blue. The polarity of the individual amino acid residues can be seen better in the <scene name='Sandbox_32/Polar_vs_non_stick/1'>stick model</scene> or the <scene name='Sandbox_32/Spacefill_polar_vs_nonpolar/2'>spacefill model</scene>. The polar amino acid residues are again shown in pink, while the non-polar amino acid residues are shown in blue. By rotating the three representations of the polar versus non-polar areas of the protein to an aerial view, it can be seen that the polar (hydrophilic) areas are located toward the outside of the protein, while the non-polar (hydrophobic) areas are located toward the inside of the protein.
-The charge of the different components of Trypsin are shown in this <scene name='Sandbox_32/Side_chains_charged/1'>charged</scene> figure. The cationic (+) atoms are shown in blue, while the anionic (-) are shown in red. These charged aspects of the protein face the outside environment surrounding the protein. The light purple parts of the protein are uncharged and the gray portions of the protein are hydrophobic. These portions of the protein make up the hydrophobic core of the protein. The charged and uncharged portions of the protein directly relate to the hydrophilic and hydrophobic character of the protein.
-The <scene name='Sandbox_32/Side_chains/1'>side chains</scene> are attached to the amino acids residues that make up the protein. In this figure the side chains of the protein are shown in pink and the rest of the protein is shown in grey. There are numerous different side chains represented on the protein. Some of the side chains are aromatic, while others are not. Some side chains are <scene name='Sandbox_32/Side_chains_charged/1'>charged</scene>, while others are uncharged. The type of side chain it is and therefore the corresponding amino acid can be determined by the charge on the side chain.
-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.
-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.
 [[Image:Tryogen.gif |thumb|left|Trypsinogen]]
@@ Line 21: / Line 6: @@
 Trypsin has many applications due to fact that it is easily purified in high quantities. The trypsin enzyme is often used in the research setting to digest proteins and then identify the resulting peptides using mass spectrometry. Trypsin has many uses in the medical field such as dissolving blood clots and treating inflammation. Other applications include its use in pre-digesting of baby food, fingerprinting and sequencing work, and environmental monitoring <ref> Trypsin. 2010. 30 October 2010 <http://www.worthington-biochem.com/tyr/default.html></ref>.
+<applet load='3ljj' size='350' frame='true' align='right' caption='Trypsin' />