Sandbox 32: Difference between revisions
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Trypsin, chymotrypsin, and elastase are all digestive enzymes that are produced in the pancreas and catalyze the hydrolysis of peptide bonds. Each of these enzymes has different specificities in regards to the side chains next to the peptide bond. Chymotrypsin prefers a large hydrophobic residue, trypsin is specific for a positively charged residue, and elastase prefers a small neutral residue. Chymotrypsin, trypsin and elastase are all proteins that contain a catalytic mechanism and hydrolyze peptides using the serine protease mechanism. Chymotrypsin and elastase are both homologs of Trypsin since they are 40% alike in structure and composition <ref> Pratt, C.W., Voet, D., Voet, J.G. Fundamentals of Biochemistry - Life at the Molecular Level - Third Edition. Voet, Voet and Pratt, 2008. </ref>. In the <scene name='Sandbox_32/Chymotrypsin/2'>Chymotrypsin</scene> structure shown the alpha helices are blue, the beta sheets are green, and the remainder of the protein is red. In the <scene name='Sandbox_32/Elastase/2'>Elastase</scene> structure shown the alpha helices are in red, the beta sheets are yellow, and the remainder of the protein is orange. | Trypsin, chymotrypsin, and elastase are all digestive enzymes that are produced in the pancreas and catalyze the hydrolysis of peptide bonds. Each of these enzymes has different specificities in regards to the side chains next to the peptide bond. Chymotrypsin prefers a large hydrophobic residue, trypsin is specific for a positively charged residue, and elastase prefers a small neutral residue. Chymotrypsin, trypsin and elastase are all proteins that contain a catalytic mechanism and hydrolyze peptides using the serine protease mechanism. Chymotrypsin and elastase are both homologs of Trypsin since they are 40% alike in structure and composition <ref> Pratt, C.W., Voet, D., Voet, J.G. Fundamentals of Biochemistry - Life at the Molecular Level - Third Edition. Voet, Voet and Pratt, 2008. </ref>. In the <scene name='Sandbox_32/Chymotrypsin/2'>Chymotrypsin</scene> structure shown the alpha helices are blue, the beta sheets are green, and the remainder of the protein is red. In the <scene name='Sandbox_32/Elastase/2'>Elastase</scene> structure shown the alpha helices are in red, the beta sheets are yellow, and the remainder of the protein is orange. | ||
==Applications and Uses of Trypsin== | ==Applications and Uses of Trypsin== | ||
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. | 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>. | ||
==References== | ==References== | ||
<references/> | <references/> | ||
