Sandbox 49: Difference between revisions

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[[Image:Lys_and_arg.gif | thumb]]

The <scene name='Sandbox_49/Ligands/1'>ligands</scene> found in trypsin are composed of oxygen(red) and sulfur (yellow). Trypsin contains four ligands and these are the areas where intermolecular forces occur, including van der Waals forces, ionic bonds and hydrogen bonds. These forces allow trypsin to bind with other molecules in order to carry out a certain process. Trypsin is active against only the peptide bonds in protein molecules that have carboxyl groups donated by the positively charged amino acids arginine and lysine (seen to the right), which are stabilized and attracted by aspartate, leading to enzyme specificity. <scene name='Sandbox_49/H20/1'>Water</scene> is an example of the van der Waals forces that are occurring with trypsin. Only a small amount of the water binds tightly enough to be seen, whereas there is much more in actuality surrounding trypsin but cannot be seen due to disorder. Trypsin is a hydrolase and cleaves bonds by hydrolysis at the peptide bonds. <scene name='Sandbox_49/Dna/1'>DNA</scene> can interact with the alpha helices and <scene name='Sandbox_49/Dna_sheet/1'>DNA</scene> can also interact with the beta sheets.

The <scene name='Sandbox_49/Ligands/1'>ligands</scene> found in trypsin are composed of oxygen(red) and sulfur (yellow). Trypsin contains four ligands and these are the areas where intermolecular forces occur, including van der Waals forces, ionic bonds and hydrogen bonds. These forces allow trypsin to bind with other molecules in order to carry out a certain process. Trypsin is active against only the peptide bonds in protein molecules that have carboxyl groups donated by the positively charged amino acids arginine and lysine (seen to the right), which are stabilized and attracted by aspartate, leading to enzyme specificity. <scene name='Sandbox_49/H20/1'>Water</scene> is an example of the van der Waals forces that are occurring with trypsin. Only a small amount of the water binds tightly enough to be seen, whereas there is much more in actuality surrounding trypsin but cannot be seen due to disorder. Trypsin is a hydrolase and cleaves bonds by hydrolysis at the peptide bonds. <scene name='Sandbox_49/Dna/1'>DNA</scene> can interact with the alpha helices and <scene name='Sandbox_49/Dna_sheet/1'>DNA</scene> can also interact with the beta sheets (nucleotide interactions).

Sandbox 49: Difference between revisions

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Revision as of 14:12, 30 October 2010 view source Student (talk \| contribs) students 33,923 edits No edit summary ← Older edit		Revision as of 14:22, 30 October 2010 view source Student (talk \| contribs) students 33,923 edits No edit summary Newer edit →
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	[[Image:Lys_and_arg.gif \| thumb]]		[[Image:Lys_and_arg.gif \| thumb]]
	The <scene name='Sandbox_49/Ligands/1'>ligands</scene> found in trypsin are composed of oxygen(red) and sulfur (yellow). Trypsin contains four ligands and these are the areas where intermolecular forces occur, including van der Waals forces, ionic bonds and hydrogen bonds. These forces allow trypsin to bind with other molecules in order to carry out a certain process. Trypsin is active against only the peptide bonds in protein molecules that have carboxyl groups donated by the positively charged amino acids arginine and lysine (seen to the right), which are stabilized and attracted by aspartate, leading to enzyme specificity. <scene name='Sandbox_49/H20/1'>Water</scene> is an example of the van der Waals forces that are occurring with trypsin. Only a small amount of the water binds tightly enough to be seen, whereas there is much more in actuality surrounding trypsin but cannot be seen due to disorder. Trypsin is a hydrolase and cleaves bonds by hydrolysis at the peptide bonds. <scene name='Sandbox_49/Dna/1'>DNA</scene> can interact with the alpha helices and <scene name='Sandbox_49/Dna_sheet/1'>DNA</scene> can also interact with the beta sheets.		The <scene name='Sandbox_49/Ligands/1'>ligands</scene> found in trypsin are composed of oxygen(red) and sulfur (yellow). Trypsin contains four ligands and these are the areas where intermolecular forces occur, including van der Waals forces, ionic bonds and hydrogen bonds. These forces allow trypsin to bind with other molecules in order to carry out a certain process. Trypsin is active against only the peptide bonds in protein molecules that have carboxyl groups donated by the positively charged amino acids arginine and lysine (seen to the right), which are stabilized and attracted by aspartate, leading to enzyme specificity. <scene name='Sandbox_49/H20/1'>Water</scene> is an example of the van der Waals forces that are occurring with trypsin. Only a small amount of the water binds tightly enough to be seen, whereas there is much more in actuality surrounding trypsin but cannot be seen due to disorder. Trypsin is a hydrolase and cleaves bonds by hydrolysis at the peptide bonds. <scene name='Sandbox_49/Dna/1'>DNA</scene> can interact with the alpha helices and <scene name='Sandbox_49/Dna_sheet/1'>DNA</scene> can also interact with the beta sheets (nucleotide interactions).