Phillips Academy Computer-Aided Protein Visualization Lab - Revision history

Jeremiah C Hagler at 20:20, 15 September 2018

2018-09-15T20:20:16Z

←Older revision		Revision as of 20:20, 15 September 2018
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	For all of the protein structures you will visualize below, once you click on the green link, the structure will appear in the structure window on the right side of the page. In the structure window, click on "Popup" button to open a larger popup window of this structure. You can toggle the spin of the structure on or off by clicking on the "Spin" button. Clicking and holding on the structure in the window will allow you to manipulate the structure, rotating in three-dimension.		For all of the protein structures you will visualize below, once you click on the green link, the structure will appear in the structure window on the right side of the page. In the structure window, click on "Popup" button to open a larger popup window of this structure. You can toggle the spin of the structure on or off by clicking on the "Spin" button. Clicking and holding on the structure in the window will allow you to manipulate the structure, rotating in three-dimension.

-	On the right side of this window you will our first example of a protein represented in three dimensions. This is protein G from the Streptococcal bacterium....a small and very simple polypeptide that binds to antibodies and messes up their organization such that their ability to further activate an immune response is hampered. As you can see in this cartoon representation of protein G, there are two main sub-structures (secondary structure) of this protein. In red is the alpha helix, while a beta sheet is in gold. The regions linking the alpha helix and beta sheets together are called turns or linking regions and are not considered to be discrete secondary structures since they are not tightly structured and tend to be floppy.	+	On the right side of this window you will our first example of a protein represented in three dimensions. This is protein G from the Streptococcal bacterium....a small and very simple polypeptide that binds to antibodies and messes up their organization such that their ability to further activate an immune response is hampered.

-	1.Alpha helix <scene name='79/795987/Pg/9'>Click to see alpha helix in relation to beta sheet</scene> Here you can see the alpha helix of protein G in red and in ball and stick representation. The beta sheet is gold, in cartoon representation. Now<scene name='79/795987/Pg/7'>click to view alpha helix in isolation</scene>. Here the alpha helix is completely isolated. The rest of the protein is hidden. The '''amino acid backbone''' (the parts of the amino acids that are linked together by a '''peptide bond''' to form the primary sequence) is shown in red. The '''amino acid side chains''' are shown in tan (each type of amino acid has its own unique side chain, one of 20 different types). ~~If a section of a protein's primary sequence of amino acids forms this coiled structure, it is known as an alpha-helix.~~	+	''Secondary Structure'': As you can see in this cartoon representation of protein G, there are two main sub-structures (secondary structure) of this protein. In red is the alpha helix, while a beta sheet is in gold. The regions linking the alpha helix and beta sheets together are called turns or linking regions (in white) and are not considered to be discrete secondary structures since they are not tightly structured and tend to be floppy.
		+
		+	1.Alpha helix <scene name='79/795987/Pg/9'>Click to see alpha helix in relation to beta sheet</scene> Here you can see the alpha helix of protein G in red and in ball and stick representation. The beta sheet is gold, in cartoon representation. Now <scene name='79/795987/Pg/7'>click to view alpha helix in isolation</scene>. Here the alpha helix is completely isolated. The rest of the protein is hidden. The '''amino acid backbone''' (the parts of the amino acids that are linked together by a '''peptide bond''' to form the primary sequence) is shown in red. The '''amino acid side chains''' are shown in tan (each type of amino acid has its own unique side chain, one of 20 different types).

-	2.Beta sheet <scene name='71/~~713432~~/~~Protein_secondary_structure_bs~~/2'>Click to see beta sheet</scene><scene name='79/795987/Pg/8'>~~Click~~ to see beta sheet in isolation</scene>	+	2.Beta sheet <scene name='79/795987/Pg/4'>Click to see the beta sheet in relation to the alpha helix</scene> Here you can see the beta sheet of protein G gold, ball and stick representation. The alpha helix is red and in cartoon representation. Now <scene name='79/795987/Pg/8'>click to see beta sheet in isolation</scene>. Here it the beta sheet is completely isolated. The rest of the protein is hidden. The amino acid backbone is in gold, the side chains in light blue.
	<br>		<br>
-	The second step of protein folding results in the '''tertiary structure''' (or 3° structure). Tertiary structure gives the protein an overall three-dimensional structure. The tertiary structure of a protein is determined by a combination of factors including hydrogen bonds, '''ionic bonds''' (between positively and negatively charged amino acids), '''covalent''' '''disulfide bonds''' (between cysteine residues), and '''Van der Waals''' interactions. Tertiary structure can also be affected by repulsive forces between similarly charged amino acids, as well as '''hydrophobic''' and '''hydrophilic''' interactions with a solvent (commonly water). At a distance many proteins form what look to be large globs at this point, and it is only upon more careful and close up inspection that one can see the true uniqueness of the shape.	+
		+	''Tertiary structure'': The second step of protein folding results in the '''tertiary structure''' (or 3° structure). Tertiary structure gives the protein an overall three-dimensional structure. The tertiary structure of a protein is determined by a combination of factors including hydrogen bonds, '''ionic bonds''' (between positively and negatively charged amino acids), '''covalent bonds''' '''disulfide bonds''' (between cysteine residues), and '''Van der Waals''' interactions. Tertiary structure can also be affected by repulsive forces between similarly charged amino acids, as well as '''hydrophobic''' and '''hydrophilic''' interactions with a solvent (commonly water). At a distance many proteins form what look to be large globs at this point, and it is only upon more careful and close up inspection that one can see the true uniqueness of the shape.
	<br>		<br>
	[[Image:Intramolecular forces in tertiary structures.png]]		[[Image:Intramolecular forces in tertiary structures.png]]
-	Figure 3: The various intramolecular interactions that help determine ~~teriary~~ structure	+	Figure 3: The various intramolecular interactions that help determine tertiary structure

	Proteins may contain only alpha helices, only beta sheets, or a combination of the two. The same holds true for the bonds giving a protein its tertiary structure - all, some or none may be present. These different folding patterns existing in different proteins are what give the proteins their distinctive shapes and sizes. A protein that is 300 amino acids long will be 100 nm as an extended chain. If the protein is an alpha helix, it will be 45 nm long; a beta sheet will be 7 x 7 x 0.8 nm; and a small globular form will form a sphere only 4.5 nm in diameter!		Proteins may contain only alpha helices, only beta sheets, or a combination of the two. The same holds true for the bonds giving a protein its tertiary structure - all, some or none may be present. These different folding patterns existing in different proteins are what give the proteins their distinctive shapes and sizes. A protein that is 300 amino acids long will be 100 nm as an extended chain. If the protein is an alpha helix, it will be 45 nm long; a beta sheet will be 7 x 7 x 0.8 nm; and a small globular form will form a sphere only 4.5 nm in diameter!

Jeremiah C Hagler at 20:01, 15 September 2018

2018-09-15T20:01:50Z

←Older revision		Revision as of 20:01, 15 September 2018
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	== Introduction to Computer-Aided Protein Visualization Lab ==		== Introduction to Computer-Aided Protein Visualization Lab ==
-	<StructureSection load='1pgb' size='340' side='right' caption='This simple protein, B1 Immunoglobulin-binding domain of Streptococcal protein G, shows secondary structures nicely. The alpha helix is red, beta sheet in yellow.'~~> <~~scene ~~name~~='79/795987/Pg/1'~~>Streptococcus protein G</scene~~>	+	<StructureSection load='1pgb' size='340' side='right' caption='This simple protein, B1 Immunoglobulin-binding domain of Streptococcal protein G, shows secondary structures nicely. The alpha helix is red, beta sheet in yellow.' scene='79/795987/Pg/1'>
	== Computer-Aided Protein Visualization Lab ==		== Computer-Aided Protein Visualization Lab ==
	Knowing the three-dimensional structure of a protein can be a very powerful tool for biologists. Much can be learned about enzyme function, interaction of molecules in your immune system, the appearance of the surface of viruses, and the interaction of ligands and receptors.		Knowing the three-dimensional structure of a protein can be a very powerful tool for biologists. Much can be learned about enzyme function, interaction of molecules in your immune system, the appearance of the surface of viruses, and the interaction of ligands and receptors.

Jeremiah C Hagler at 19:55, 15 September 2018

2018-09-15T19:55:44Z

←Older revision		Revision as of 19:55, 15 September 2018
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	On the right side of this window you will our first example of a protein represented in three dimensions. This is protein G from the Streptococcal bacterium....a small and very simple polypeptide that binds to antibodies and messes up their organization such that their ability to further activate an immune response is hampered. As you can see in this cartoon representation of protein G, there are two main sub-structures (secondary structure) of this protein. In red is the alpha helix, while a beta sheet is in gold. The regions linking the alpha helix and beta sheets together are called turns or linking regions and are not considered to be discrete secondary structures since they are not tightly structured and tend to be floppy.		On the right side of this window you will our first example of a protein represented in three dimensions. This is protein G from the Streptococcal bacterium....a small and very simple polypeptide that binds to antibodies and messes up their organization such that their ability to further activate an immune response is hampered. As you can see in this cartoon representation of protein G, there are two main sub-structures (secondary structure) of this protein. In red is the alpha helix, while a beta sheet is in gold. The regions linking the alpha helix and beta sheets together are called turns or linking regions and are not considered to be discrete secondary structures since they are not tightly structured and tend to be floppy.

-	1.Alpha helix <scene name='79/795987/Pg/9'>Click to see alpha helix in relation to beta sheet</scene> Here you can see the alpha helix of protein G in red and in ball and stick representation. The beta sheet is gold, in cartoon representation. Now ~~<scene name='79/795987/Pg/5'>~~<scene name='79/795987/Pg/7'>click to view alpha helix in isolation</scene>. Here the alpha helix is completely isolated. The rest of the protein is hidden. The '''amino acid backbone''' (the parts of the amino acids that are linked together by a '''peptide bond''' to form the primary sequence) is shown in red. The '''amino acid side chains''' are shown in tan (each type of amino acid has its own unique side chain, one of 20 different types). If a section of a protein's primary sequence of amino acids forms this coiled structure, it is known as an alpha-helix.	+	1.Alpha helix <scene name='79/795987/Pg/9'>Click to see alpha helix in relation to beta sheet</scene> Here you can see the alpha helix of protein G in red and in ball and stick representation. The beta sheet is gold, in cartoon representation. Now<scene name='79/795987/Pg/7'>click to view alpha helix in isolation</scene>. Here the alpha helix is completely isolated. The rest of the protein is hidden. The '''amino acid backbone''' (the parts of the amino acids that are linked together by a '''peptide bond''' to form the primary sequence) is shown in red. The '''amino acid side chains''' are shown in tan (each type of amino acid has its own unique side chain, one of 20 different types). If a section of a protein's primary sequence of amino acids forms this coiled structure, it is known as an alpha-helix.

	2.Beta sheet <scene name='71/713432/Protein_secondary_structure_bs/2'>Click to see beta sheet</scene><scene name='79/795987/Pg/8'>Click to see beta sheet in isolation</scene>		2.Beta sheet <scene name='71/713432/Protein_secondary_structure_bs/2'>Click to see beta sheet</scene><scene name='79/795987/Pg/8'>Click to see beta sheet in isolation</scene>

Jeremiah C Hagler at 19:54, 15 September 2018

2018-09-15T19:54:39Z

←Older revision		Revision as of 19:54, 15 September 2018
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	== Introduction to Computer-Aided Protein Visualization Lab ==		== Introduction to Computer-Aided Protein Visualization Lab ==
-	<StructureSection load='1pgb' size='340' side='right' caption='This simple protein, B1 Immunoglobulin-binding domain of Streptococcal protein G, shows secondary structures nicely. The alpha helix is red, beta sheet in yellow.~~' scene='71/713432/Protein_secondary_structure/1~~'> <scene name='79/795987/Pg/1'>Streptococcus protein G</scene>	+	<StructureSection load='1pgb' size='340' side='right' caption='This simple protein, B1 Immunoglobulin-binding domain of Streptococcal protein G, shows secondary structures nicely. The alpha helix is red, beta sheet in yellow.'> <scene name='79/795987/Pg/1'>Streptococcus protein G</scene>
	== Computer-Aided Protein Visualization Lab ==		== Computer-Aided Protein Visualization Lab ==
	Knowing the three-dimensional structure of a protein can be a very powerful tool for biologists. Much can be learned about enzyme function, interaction of molecules in your immune system, the appearance of the surface of viruses, and the interaction of ligands and receptors.		Knowing the three-dimensional structure of a protein can be a very powerful tool for biologists. Much can be learned about enzyme function, interaction of molecules in your immune system, the appearance of the surface of viruses, and the interaction of ligands and receptors.

Jeremiah C Hagler at 19:52, 15 September 2018

2018-09-15T19:52:05Z

←Older revision		Revision as of 19:52, 15 September 2018
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	Protein folding:		Protein folding:

-	The most important rule about protein structure is that it is determined by the primary sequence of the protein. Protein folding is a complicated multi-step process. The first step results in the '''secondary structure''' (or 2o structure) of the protein. Secondary structures come in two flavors: '''alpha helices''' and '''beta sheets''' (or beta-pleated sheets). Alpha helices are spiral staircase structures (see structure 1 below), and beta-pleated sheets are flat regions where the amino acids run back and forth next to each other in long ribbons (see structure 2 below). These two structures form spontaneously based on the shape/'''hydrophobicity'''/'''charges''' of the amino acids and are held together by '''hydrogen bonds'''. The protein will now look like a string of pearls with twists or zig-zags at intervals along its length.	+	The most important rule about protein structure is that it is determined by the primary sequence of the protein. Protein folding is a complicated multi-step process. The first step results in the '''secondary structure''' (or 2° structure) of the protein. Secondary structures come in two flavors: '''alpha helices''' and '''beta sheets''' (or beta-pleated sheets). Alpha helices are spiral staircase structures (see structure 1 below), and beta-pleated sheets are flat regions where the amino acids run back and forth next to each other in long ribbons (see structure 2 below). These two structures form spontaneously based on the shape/'''hydrophobicity'''/'''charges''' of the amino acids and are held together by '''hydrogen bonds'''. The protein will now look like a string of pearls with twists or zig-zags at intervals along its length.

-	1. <scene name='71/713432/Protein_secondary_structure/3'>Click to see alpha helix</scene> <scene name='79/795987/Pg/9'>Click to see alpha helix in relation to beta sheet</scene><scene name='79/795987/Pg/5'>Click to see alpha helix highlighted</scene>In the structure window, click on "Popup" button to open a larger popup window of this structure. You can toggle the spin of the structure on or off by clicking on the "Spin" button. Clicking and holding on the structure in the window will allow you to manipulate the structure, rotating in three-~~dimensions.~~	+	For all of the protein structures you will visualize below, once you click on the green link, the structure will appear in the structure window on the right side of the page. In the structure window, click on "Popup" button to open a larger popup window of this structure. You can toggle the spin of the structure on or off by clicking on the "Spin" button. Clicking and holding on the structure in the window will allow you to manipulate the structure, rotating in three-dimension.
-		+
-	This is an alpha helix. The '''amino acid backbone''' (the parts of the amino acids that are linked together by a '''peptide bond''' to form the 1o sequence) is shown in pink/red. The '''amino acid side chains''' are shown in yellow (each type of amino acid has its own unique side chain, one of 20 different types). If a section of a protein's primary sequence of amino acids forms this coiled structure, it is known as an alpha-helix.	+

-	~~[Put in manipulations of cartoon view to stick, backbone only then backbone with~~ side ~~chains~~.....~~..adjust color scheme~~ to ~~emphasize~~ secondary structure. ~~Isolate~~ secondary structures ~~if possible~~, ~~etc]~~	+	On the right side of this window you will our first example of a protein represented in three dimensions. This is protein G from the Streptococcal bacterium....a small and very simple polypeptide that binds to antibodies and messes up their organization such that their ability to further activate an immune response is hampered. As you can see in this cartoon representation of protein G, there are two main sub-structures (secondary structure) of this protein. In red is the alpha helix, while a beta sheet is in gold. The regions linking the alpha helix and beta sheets together are called turns or linking regions and are not considered to be discrete secondary structures since they are not tightly structured and tend to be floppy.
-		+
-	2. <scene name='71/713432/Protein_secondary_structure_bs/2'>Click to see beta sheet</scene><scene name='79/795987/Pg/8'>Click to see beta sheet in isolation</scene>	+	1.Alpha helix <scene name='79/795987/Pg/9'>Click to see alpha helix in relation to beta sheet</scene> Here you can see the alpha helix of protein G in red and in ball and stick representation. The beta sheet is gold, in cartoon representation. Now <scene name='79/795987/Pg/5'><scene name='79/795987/Pg/7'>click to view alpha helix in isolation</scene>. Here the alpha helix is completely isolated. The rest of the protein is hidden. The '''amino acid backbone''' (the parts of the amino acids that are linked together by a '''peptide bond''' to form the primary sequence) is shown in red. The '''amino acid side chains''' are shown in tan (each type of amino acid has its own unique side chain, one of 20 different types). If a section of a protein's primary sequence of amino acids forms this coiled structure, it is known as an alpha-helix.
		+
		+	2.Beta sheet <scene name='71/713432/Protein_secondary_structure_bs/2'>Click to see beta sheet</scene><scene name='79/795987/Pg/8'>Click to see beta sheet in isolation</scene>
	<br>		<br>
	The second step of protein folding results in the '''tertiary structure''' (or 3° structure). Tertiary structure gives the protein an overall three-dimensional structure. The tertiary structure of a protein is determined by a combination of factors including hydrogen bonds, '''ionic bonds''' (between positively and negatively charged amino acids), '''covalent''' '''disulfide bonds''' (between cysteine residues), and '''Van der Waals''' interactions. Tertiary structure can also be affected by repulsive forces between similarly charged amino acids, as well as '''hydrophobic''' and '''hydrophilic''' interactions with a solvent (commonly water). At a distance many proteins form what look to be large globs at this point, and it is only upon more careful and close up inspection that one can see the true uniqueness of the shape.		The second step of protein folding results in the '''tertiary structure''' (or 3° structure). Tertiary structure gives the protein an overall three-dimensional structure. The tertiary structure of a protein is determined by a combination of factors including hydrogen bonds, '''ionic bonds''' (between positively and negatively charged amino acids), '''covalent''' '''disulfide bonds''' (between cysteine residues), and '''Van der Waals''' interactions. Tertiary structure can also be affected by repulsive forces between similarly charged amino acids, as well as '''hydrophobic''' and '''hydrophilic''' interactions with a solvent (commonly water). At a distance many proteins form what look to be large globs at this point, and it is only upon more careful and close up inspection that one can see the true uniqueness of the shape.

Jeremiah C Hagler at 18:56, 15 September 2018

2018-09-15T18:56:50Z

←Older revision		Revision as of 18:56, 15 September 2018
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	The most important rule about protein structure is that it is determined by the primary sequence of the protein. Protein folding is a complicated multi-step process. The first step results in the '''secondary structure''' (or 2o structure) of the protein. Secondary structures come in two flavors: '''alpha helices''' and '''beta sheets''' (or beta-pleated sheets). Alpha helices are spiral staircase structures (see structure 1 below), and beta-pleated sheets are flat regions where the amino acids run back and forth next to each other in long ribbons (see structure 2 below). These two structures form spontaneously based on the shape/'''hydrophobicity'''/'''charges''' of the amino acids and are held together by '''hydrogen bonds'''. The protein will now look like a string of pearls with twists or zig-zags at intervals along its length.		The most important rule about protein structure is that it is determined by the primary sequence of the protein. Protein folding is a complicated multi-step process. The first step results in the '''secondary structure''' (or 2o structure) of the protein. Secondary structures come in two flavors: '''alpha helices''' and '''beta sheets''' (or beta-pleated sheets). Alpha helices are spiral staircase structures (see structure 1 below), and beta-pleated sheets are flat regions where the amino acids run back and forth next to each other in long ribbons (see structure 2 below). These two structures form spontaneously based on the shape/'''hydrophobicity'''/'''charges''' of the amino acids and are held together by '''hydrogen bonds'''. The protein will now look like a string of pearls with twists or zig-zags at intervals along its length.

-	1. <scene name='71/713432/Protein_secondary_structure/3'>Click to see alpha helix</scene> In the structure window, click on "Popup" button to open a larger popup window of this structure. You can toggle the spin of the structure on or off by clicking on the "Spin" button. Clicking and holding on the structure in the window will allow you to manipulate the structure, rotating in three-dimensions.	+	1. <scene name='71/713432/Protein_secondary_structure/3'>Click to see alpha helix</scene> <scene name='79/795987/Pg/9'>Click to see alpha helix in relation to beta sheet</scene><scene name='79/795987/Pg/5'>Click to see alpha helix highlighted</scene>In the structure window, click on "Popup" button to open a larger popup window of this structure. You can toggle the spin of the structure on or off by clicking on the "Spin" button. Clicking and holding on the structure in the window will allow you to manipulate the structure, rotating in three-dimensions.

	This is an alpha helix. The '''amino acid backbone''' (the parts of the amino acids that are linked together by a '''peptide bond''' to form the 1o sequence) is shown in pink/red. The '''amino acid side chains''' are shown in yellow (each type of amino acid has its own unique side chain, one of 20 different types). If a section of a protein's primary sequence of amino acids forms this coiled structure, it is known as an alpha-helix.		This is an alpha helix. The '''amino acid backbone''' (the parts of the amino acids that are linked together by a '''peptide bond''' to form the 1o sequence) is shown in pink/red. The '''amino acid side chains''' are shown in yellow (each type of amino acid has its own unique side chain, one of 20 different types). If a section of a protein's primary sequence of amino acids forms this coiled structure, it is known as an alpha-helix.

Jeremiah C Hagler at 18:46, 15 September 2018

2018-09-15T18:46:57Z

←Older revision		Revision as of 18:46, 15 September 2018
Line 18:		Line 18:
	[Put in manipulations of cartoon view to stick, backbone only then backbone with side chains.......adjust color scheme to emphasize secondary structure. Isolate secondary structures if possible, etc]		[Put in manipulations of cartoon view to stick, backbone only then backbone with side chains.......adjust color scheme to emphasize secondary structure. Isolate secondary structures if possible, etc]

-	2. <scene name='71/713432/Protein_secondary_structure_bs/2'>Click to see beta sheet</scene>	+	2. <scene name='71/713432/Protein_secondary_structure_bs/2'>Click to see beta sheet</scene><scene name='79/795987/Pg/8'>Click to see beta sheet in isolation</scene>
	<br>		<br>
	The second step of protein folding results in the '''tertiary structure''' (or 3° structure). Tertiary structure gives the protein an overall three-dimensional structure. The tertiary structure of a protein is determined by a combination of factors including hydrogen bonds, '''ionic bonds''' (between positively and negatively charged amino acids), '''covalent''' '''disulfide bonds''' (between cysteine residues), and '''Van der Waals''' interactions. Tertiary structure can also be affected by repulsive forces between similarly charged amino acids, as well as '''hydrophobic''' and '''hydrophilic''' interactions with a solvent (commonly water). At a distance many proteins form what look to be large globs at this point, and it is only upon more careful and close up inspection that one can see the true uniqueness of the shape.		The second step of protein folding results in the '''tertiary structure''' (or 3° structure). Tertiary structure gives the protein an overall three-dimensional structure. The tertiary structure of a protein is determined by a combination of factors including hydrogen bonds, '''ionic bonds''' (between positively and negatively charged amino acids), '''covalent''' '''disulfide bonds''' (between cysteine residues), and '''Van der Waals''' interactions. Tertiary structure can also be affected by repulsive forces between similarly charged amino acids, as well as '''hydrophobic''' and '''hydrophilic''' interactions with a solvent (commonly water). At a distance many proteins form what look to be large globs at this point, and it is only upon more careful and close up inspection that one can see the true uniqueness of the shape.

Jeremiah C Hagler at 18:01, 15 September 2018

2018-09-15T18:01:44Z

←Older revision		Revision as of 18:01, 15 September 2018
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	== Introduction to Computer-Aided Protein Visualization Lab ==		== Introduction to Computer-Aided Protein Visualization Lab ==
-	<StructureSection load='1pgb' size='340' side='right' caption='This simple protein, B1 Immunoglobulin-binding domain of Streptococcal protein G, shows secondary structures nicely. The alpha helix is red, beta sheet in yellow.' scene='71/713432/Protein_secondary_structure/1'>	+	<StructureSection load='1pgb' size='340' side='right' caption='This simple protein, B1 Immunoglobulin-binding domain of Streptococcal protein G, shows secondary structures nicely. The alpha helix is red, beta sheet in yellow.' scene='71/713432/Protein_secondary_structure/1'> <scene name='79/795987/Pg/1'>Streptococcus protein G</scene>
	== Computer-Aided Protein Visualization Lab ==		== Computer-Aided Protein Visualization Lab ==
	Knowing the three-dimensional structure of a protein can be a very powerful tool for biologists. Much can be learned about enzyme function, interaction of molecules in your immune system, the appearance of the surface of viruses, and the interaction of ligands and receptors.		Knowing the three-dimensional structure of a protein can be a very powerful tool for biologists. Much can be learned about enzyme function, interaction of molecules in your immune system, the appearance of the surface of viruses, and the interaction of ligands and receptors.

Jeremiah C Hagler at 17:51, 15 September 2018

2018-09-15T17:51:54Z

←Older revision		Revision as of 17:51, 15 September 2018
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	2.[http://proteopedia.org/wiki/index.php/User:Jeremiah_C_Hagler/Sandbox_3 Protein 3: HIV Reverse Transcriptase]		2.[http://proteopedia.org/wiki/index.php/User:Jeremiah_C_Hagler/Sandbox_3 Protein 3: HIV Reverse Transcriptase]
	<br>		<br>
-	3.[http://proteopedia.org/wiki/index.php/User:Jeremiah_C_Hagler/Sandbox_1 Protein 2: Alkaline Phosphatase]	+	3.[http://proteopedia.org/wiki/index.php/User:Jeremiah_C_Hagler/Sandbox_1 Protein 2: Alkaline Phosphatase] <scene name='79/795987/Ap/1'>Alkaline Phosphatase</scene>
	<br>		<br>

	<references/>		<references/>

Jeremiah C Hagler: User:Jeremiah C Hagler/Protein 1 Modified moved to Phillips Academy Computer-Aided Protein Visualization Lab

2018-09-15T17:45:07Z

User:Jeremiah C Hagler/Protein 1 Modified moved to Phillips Academy Computer-Aided Protein Visualization Lab

←Older revision

Revision as of 17:45, 15 September 2018