User:Thomas McNamara/Sandbox 1 - Revision history

Thomas McNamara at 00:18, 17 December 2018

Thomas McNamara — Mon, 17 Dec 2018 00:18:02 GMT

←Older revision		Revision as of 00:18, 17 December 2018
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	Each Immunoglobulin G protein is made of four separate peptide chains --<scene name='80/803917/Immunoglobulin_g/1'> two identical longer chains, called heavy chains, and two identical smaller chains, called light chains.</scene> Together, these four chains come together to form a Y-shaped molecule, with the two binding sites forming at the end of each arm. At a more in-depth look, one can see that each light chain consists of two domains, a variable region and a constant region; while each heavy chain consists of 4 domains, one variable region and three constant regions. Structurally, each domain of each peptide is made up of <scene name='80/803917/Individual_domain_structure/1'>two beta-sheets, pinned together by a disulfide bridge in the middle</scene>. While the disulfide bond provides extra stability, the hydrophobic effect is the driving force behind this structural conformation, with the side chains of each hydrophobic amino acid oriented towards to middle of the 'beta-sheet sandwich.' Additionally, in the constant domains, hydrophilic amino acids orient their side chains outwards so that they can interact with other molecules, such as immune receptors that facilitate the next step in the pathogen degradation pathway. This also hints at the need for each constant domain to retain its amino acid sequence between each Immunoglobulin G protein, as all of these proteins must still bind to immune receptors, despite the pathogen bound.		Each Immunoglobulin G protein is made of four separate peptide chains --<scene name='80/803917/Immunoglobulin_g/1'> two identical longer chains, called heavy chains, and two identical smaller chains, called light chains.</scene> Together, these four chains come together to form a Y-shaped molecule, with the two binding sites forming at the end of each arm. At a more in-depth look, one can see that each light chain consists of two domains, a variable region and a constant region; while each heavy chain consists of 4 domains, one variable region and three constant regions. Structurally, each domain of each peptide is made up of <scene name='80/803917/Individual_domain_structure/1'>two beta-sheets, pinned together by a disulfide bridge in the middle</scene>. While the disulfide bond provides extra stability, the hydrophobic effect is the driving force behind this structural conformation, with the side chains of each hydrophobic amino acid oriented towards to middle of the 'beta-sheet sandwich.' Additionally, in the constant domains, hydrophilic amino acids orient their side chains outwards so that they can interact with other molecules, such as immune receptors that facilitate the next step in the pathogen degradation pathway. This also hints at the need for each constant domain to retain its amino acid sequence between each Immunoglobulin G protein, as all of these proteins must still bind to immune receptors, despite the pathogen bound.

-	Notably, the two <scene name='80/803917/Individual_domain_structure/4'>antigen binding pockets are formed at the interface between the light and heavy chains' variable domains</scene>. Within each antibody's variable domain are three loops, referred to as hypervariable regions or complimentary determining regions, that differ in amino acid sequence between each Immunoglobulin G protein. Ultimately, it is the amino acid sequence of each of these loops (and therefore the length and conformation of each loop) and the juxtaposition of the six loops coming together that give each antibody a very unique binding pocket. The largest of the three loops, often referred to as H3, is located at the center of the antigen binding site, blocking access in the unliganded form.	+	Notably, the two <scene name='80/803917/Individual_domain_structure/4'>antigen binding pockets are formed at the interface between the light and heavy chains' variable domains</scene>. Within each antibody's variable domain are three loops, referred to as hypervariable regions or complimentary determining regions, that differ in amino acid sequence between each Immunoglobulin G protein. Ultimately, <scene name='80/803917/Antigen_binding_site/1'>it is the amino acid sequence of each of these loops (and therefore the length and conformation of each loop) and the juxtaposition of the six loops coming together that give each antibody a very unique binding pocket</scene>. The largest of the three loops, often referred to as H3, is located at the center of the antigen binding site, blocking access in the unliganded form.

	==References==		==References==

Thomas McNamara at 00:12, 17 December 2018

Thomas McNamara — Mon, 17 Dec 2018 00:12:10 GMT

←Older revision		Revision as of 00:12, 17 December 2018
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	Notably, the two <scene name='80/803917/Individual_domain_structure/4'>antigen binding pockets are formed at the interface between the light and heavy chains' variable domains</scene>. Within each antibody's variable domain are three loops, referred to as hypervariable regions or complimentary determining regions, that differ in amino acid sequence between each Immunoglobulin G protein. Ultimately, it is the amino acid sequence of each of these loops (and therefore the length and conformation of each loop) and the juxtaposition of the six loops coming together that give each antibody a very unique binding pocket. The largest of the three loops, often referred to as H3, is located at the center of the antigen binding site, blocking access in the unliganded form.		Notably, the two <scene name='80/803917/Individual_domain_structure/4'>antigen binding pockets are formed at the interface between the light and heavy chains' variable domains</scene>. Within each antibody's variable domain are three loops, referred to as hypervariable regions or complimentary determining regions, that differ in amino acid sequence between each Immunoglobulin G protein. Ultimately, it is the amino acid sequence of each of these loops (and therefore the length and conformation of each loop) and the juxtaposition of the six loops coming together that give each antibody a very unique binding pocket. The largest of the three loops, often referred to as H3, is located at the center of the antigen binding site, blocking access in the unliganded form.
		+
		+	==References==
		+
		+	Harris, L. J., Larson, S. B., Hasel, K. W., and McPherson, A. (1997) Refined Structure of an Intact IgG2a Monoclonal Antibody,. Biochemistry. 36, 1581–1597
		+
		+	Stanfield, R. L., Takimoto-Kamimura, M., Rini, J. M., Profy, A. T., and Wilson, I. A. (1993) Major antigen-induced domain rearrangements in an antibody. Structure. 10.1016/0969-2126(93)90024-B
		+
		+	Paul, W. (2013) Fundamental Immunology. 7, 129-149

Thomas McNamara at 00:03, 17 December 2018

Thomas McNamara — Mon, 17 Dec 2018 00:03:24 GMT

←Older revision		Revision as of 00:03, 17 December 2018
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	== Structural highlights ==		== Structural highlights ==

-	Each Immunoglobulin G protein is made of four separate peptide chains --<scene name='80/803917/Immunoglobulin_g/1'> two identical longer chains, called heavy chains, and two identical smaller chains, called light chains.</scene> Together, these four chains come together to form a Y-shaped molecule, with the two binding sites forming at the end of each arm. At a more in-depth look, one can see that each light chain consists of two domains, a variable region and a constant region; while each heavy chain consists of 4 domains, one variable region and three constant regions. Structurally, each domain of each peptide is made up of two beta-sheets, pinned together by a disulfide bridge in the middle. While the disulfide bond provides extra stability, the hydrophobic effect is the driving force behind this structural conformation, with the side chains of each hydrophobic amino acid oriented towards to middle of the 'beta-sheet sandwich.' Additionally, in the constant domains, hydrophilic amino acids orient their side chains outwards so that they can interact with other molecules, such as immune receptors that facilitate the next step in the pathogen degradation pathway. This also hints at the need for each constant domain to retain its amino acid sequence between each Immunoglobulin G protein, as all of these proteins must still bind to immune receptors, despite the pathogen bound.	+	Each Immunoglobulin G protein is made of four separate peptide chains --<scene name='80/803917/Immunoglobulin_g/1'> two identical longer chains, called heavy chains, and two identical smaller chains, called light chains.</scene> Together, these four chains come together to form a Y-shaped molecule, with the two binding sites forming at the end of each arm. At a more in-depth look, one can see that each light chain consists of two domains, a variable region and a constant region; while each heavy chain consists of 4 domains, one variable region and three constant regions. Structurally, each domain of each peptide is made up of <scene name='80/803917/Individual_domain_structure/1'>two beta-sheets, pinned together by a disulfide bridge in the middle</scene>. While the disulfide bond provides extra stability, the hydrophobic effect is the driving force behind this structural conformation, with the side chains of each hydrophobic amino acid oriented towards to middle of the 'beta-sheet sandwich.' Additionally, in the constant domains, hydrophilic amino acids orient their side chains outwards so that they can interact with other molecules, such as immune receptors that facilitate the next step in the pathogen degradation pathway. This also hints at the need for each constant domain to retain its amino acid sequence between each Immunoglobulin G protein, as all of these proteins must still bind to immune receptors, despite the pathogen bound.

-	Notably, the two antigen binding pockets are formed at the interface between the light and heavy chains' variable domains. Within each antibody's variable domain are three loops, referred to as hypervariable regions or complimentary determining regions, that differ in amino acid sequence between each Immunoglobulin G protein. Ultimately, it is the amino acid sequence of each of these loops (and therefore the length and conformation of each loop) and the juxtaposition of the six loops coming together that give each antibody a very unique binding pocket. The largest of the three loops, often referred to as H3, is located at the center of the antigen binding site, blocking access in the unliganded form.	+	Notably, the two <scene name='80/803917/Individual_domain_structure/4'>antigen binding pockets are formed at the interface between the light and heavy chains' variable domains</scene>. Within each antibody's variable domain are three loops, referred to as hypervariable regions or complimentary determining regions, that differ in amino acid sequence between each Immunoglobulin G protein. Ultimately, it is the amino acid sequence of each of these loops (and therefore the length and conformation of each loop) and the juxtaposition of the six loops coming together that give each antibody a very unique binding pocket. The largest of the three loops, often referred to as H3, is located at the center of the antigen binding site, blocking access in the unliganded form.

Thomas McNamara at 23:27, 16 December 2018

Thomas McNamara — Sun, 16 Dec 2018 23:27:30 GMT

←Older revision		Revision as of 23:27, 16 December 2018
Line 31:		Line 31:
	== Structural highlights ==		== Structural highlights ==

-	Each Immunoglobulin G protein is made of four separate peptide chains -- two identical longer chains, called heavy chains, and two identical smaller chains, called light chains. Together, these four chains come together to form a Y-shaped molecule, with the two binding sites forming at the end of each arm. At a more in-depth look, one can see that each light chain consists of two domains, a variable region and a constant region; while each heavy chain consists of 4 domains, one variable region and three constant regions. Structurally, each domain of each peptide is made up of two beta-sheets, pinned together by a disulfide bridge in the middle. While the disulfide bond provides extra stability, the hydrophobic effect is the driving force behind this structural conformation, with the side chains of each hydrophobic amino acid oriented towards to middle of the 'beta-sheet sandwich.' Additionally, in the constant domains, hydrophilic amino acids orient their side chains outwards so that they can interact with other molecules, such as immune receptors that facilitate the next step in the pathogen degradation pathway. This also hints at the need for each constant domain to retain its amino acid sequence between each Immunoglobulin G protein, as all of these proteins must still bind to immune receptors, despite the pathogen bound.	+	Each Immunoglobulin G protein is made of four separate peptide chains --<scene name='80/803917/Immunoglobulin_g/1'> two identical longer chains, called heavy chains, and two identical smaller chains, called light chains.</scene> Together, these four chains come together to form a Y-shaped molecule, with the two binding sites forming at the end of each arm. At a more in-depth look, one can see that each light chain consists of two domains, a variable region and a constant region; while each heavy chain consists of 4 domains, one variable region and three constant regions. Structurally, each domain of each peptide is made up of two beta-sheets, pinned together by a disulfide bridge in the middle. While the disulfide bond provides extra stability, the hydrophobic effect is the driving force behind this structural conformation, with the side chains of each hydrophobic amino acid oriented towards to middle of the 'beta-sheet sandwich.' Additionally, in the constant domains, hydrophilic amino acids orient their side chains outwards so that they can interact with other molecules, such as immune receptors that facilitate the next step in the pathogen degradation pathway. This also hints at the need for each constant domain to retain its amino acid sequence between each Immunoglobulin G protein, as all of these proteins must still bind to immune receptors, despite the pathogen bound.

	Notably, the two antigen binding pockets are formed at the interface between the light and heavy chains' variable domains. Within each antibody's variable domain are three loops, referred to as hypervariable regions or complimentary determining regions, that differ in amino acid sequence between each Immunoglobulin G protein. Ultimately, it is the amino acid sequence of each of these loops (and therefore the length and conformation of each loop) and the juxtaposition of the six loops coming together that give each antibody a very unique binding pocket. The largest of the three loops, often referred to as H3, is located at the center of the antigen binding site, blocking access in the unliganded form.		Notably, the two antigen binding pockets are formed at the interface between the light and heavy chains' variable domains. Within each antibody's variable domain are three loops, referred to as hypervariable regions or complimentary determining regions, that differ in amino acid sequence between each Immunoglobulin G protein. Ultimately, it is the amino acid sequence of each of these loops (and therefore the length and conformation of each loop) and the juxtaposition of the six loops coming together that give each antibody a very unique binding pocket. The largest of the three loops, often referred to as H3, is located at the center of the antigen binding site, blocking access in the unliganded form.

Thomas McNamara at 23:21, 16 December 2018

Thomas McNamara — Sun, 16 Dec 2018 23:21:40 GMT

←Older revision		Revision as of 23:21, 16 December 2018
Line 31:		Line 31:
	== Structural highlights ==		== Structural highlights ==

-	Each Immunoglobulin G protein is made of four separate peptide chains -- two identical longer chains, called heavy chains, and two identical smaller chains, called light chains. Together, these four chains come together to form a Y-shaped molecule, with the two binding sites forming at the end of each arm. At a more in-depth look, one can see that each light chain consists of two domains, a variable region and a constant region; while each heavy chain consists of 4 domains, one variable region and three constant regions. Structurally, each domain of each peptide is made up of two beta-sheets, pinned together by a disulfide bridge in the middle. While the disulfide bond provides extra stability, the hydrophobic effect is the driving force behind this structural conformation, with the side chains of each hydrophobic amino acid oriented towards to middle of the 'beta-sheet sandwich.' Additionally, in the constant domains, hydrophilic amino acids orient their side chains outwards so that they can interact with other molecules, such as immune receptors that facilitate the next step in the pathogen degradation pathway.	+	Each Immunoglobulin G protein is made of four separate peptide chains -- two identical longer chains, called heavy chains, and two identical smaller chains, called light chains. Together, these four chains come together to form a Y-shaped molecule, with the two binding sites forming at the end of each arm. At a more in-depth look, one can see that each light chain consists of two domains, a variable region and a constant region; while each heavy chain consists of 4 domains, one variable region and three constant regions. Structurally, each domain of each peptide is made up of two beta-sheets, pinned together by a disulfide bridge in the middle. While the disulfide bond provides extra stability, the hydrophobic effect is the driving force behind this structural conformation, with the side chains of each hydrophobic amino acid oriented towards to middle of the 'beta-sheet sandwich.' Additionally, in the constant domains, hydrophilic amino acids orient their side chains outwards so that they can interact with other molecules, such as immune receptors that facilitate the next step in the pathogen degradation pathway. This also hints at the need for each constant domain to retain its amino acid sequence between each Immunoglobulin G protein, as all of these proteins must still bind to immune receptors, despite the pathogen bound.

-	Notably, the two antigen binding pockets are formed at the interface between the light and heavy chains' variable domains. Within each antibody's variable domain are three loops, referred to as hypervariable regions or complimentary determining regions, that differ in amino acid sequence between each Immunoglobulin G protein. Ultimately, it is the amino acid sequence of each of these loops (and therefore the length and conformation of each loop) and the juxtaposition of the six loops coming together that give each antibody a very unique binding pocket.	+	Notably, the two antigen binding pockets are formed at the interface between the light and heavy chains' variable domains. Within each antibody's variable domain are three loops, referred to as hypervariable regions or complimentary determining regions, that differ in amino acid sequence between each Immunoglobulin G protein. Ultimately, it is the amino acid sequence of each of these loops (and therefore the length and conformation of each loop) and the juxtaposition of the six loops coming together that give each antibody a very unique binding pocket. The largest of the three loops, often referred to as H3, is located at the center of the antigen binding site, blocking access in the unliganded form.

Thomas McNamara at 23:14, 16 December 2018

Thomas McNamara — Sun, 16 Dec 2018 23:14:27 GMT

←Older revision		Revision as of 23:14, 16 December 2018
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	== Function ==		== Function ==

-	When a foreign pathogen invades a host organism, it is constantly coming into contact with circulating B-cells. Eventually, one particular B-cell will contain a membrane protein that recognizes and binds to a very specific region on the pathogen, called an epitope. This B-cell will then begin secreting identical Immunoglobulin G proteins whose binding sites recognize only the particular epitope. The secreted antibodies will then circulate throughout the host organism, searching for and binding to any other identical pathogens that display the same epitope. Once bound to the pathogen, the Immunoglobulin G protein can ~~either~~:	+	When a foreign pathogen invades a host organism, it is constantly coming into contact with circulating B-cells. Eventually, one particular B-cell will contain a membrane protein that recognizes and binds to a very specific region on the pathogen, called an epitope. This B-cell will then begin secreting identical Immunoglobulin G proteins whose binding sites recognize only the particular epitope. The secreted antibodies will then circulate throughout the host organism, searching for and binding to any other identical pathogens that display the same epitope. Once bound to the pathogen, the Immunoglobulin G protein can:

	1) Neutralize/Immobilize the pathogen, preventing it from functioning; and/or		1) Neutralize/Immobilize the pathogen, preventing it from functioning; and/or
Line 30:		Line 30:

	== Structural highlights ==		== Structural highlights ==
		+
		+	Each Immunoglobulin G protein is made of four separate peptide chains -- two identical longer chains, called heavy chains, and two identical smaller chains, called light chains. Together, these four chains come together to form a Y-shaped molecule, with the two binding sites forming at the end of each arm. At a more in-depth look, one can see that each light chain consists of two domains, a variable region and a constant region; while each heavy chain consists of 4 domains, one variable region and three constant regions. Structurally, each domain of each peptide is made up of two beta-sheets, pinned together by a disulfide bridge in the middle. While the disulfide bond provides extra stability, the hydrophobic effect is the driving force behind this structural conformation, with the side chains of each hydrophobic amino acid oriented towards to middle of the 'beta-sheet sandwich.' Additionally, in the constant domains, hydrophilic amino acids orient their side chains outwards so that they can interact with other molecules, such as immune receptors that facilitate the next step in the pathogen degradation pathway.
		+
		+	Notably, the two antigen binding pockets are formed at the interface between the light and heavy chains' variable domains. Within each antibody's variable domain are three loops, referred to as hypervariable regions or complimentary determining regions, that differ in amino acid sequence between each Immunoglobulin G protein. Ultimately, it is the amino acid sequence of each of these loops (and therefore the length and conformation of each loop) and the juxtaposition of the six loops coming together that give each antibody a very unique binding pocket.

Thomas McNamara at 22:41, 16 December 2018

Thomas McNamara — Sun, 16 Dec 2018 22:41:22 GMT

←Older revision		Revision as of 22:41, 16 December 2018
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	== Disease ==		== Disease ==
		+
		+	Through evolution, organisms have developed antibody-secreting immune systems that do not recognize host proteins/tissues. In rare cases, though, an organism will develop a mutation that leads to their Immunoglobulin G proteins binding to their own cells, causing the host's immune system to attack the host's healthy cells/tissues. This problem is the root of many common auto-immune diseases prevalent today.
		+

	== Relevance ==		== Relevance ==

-	~~== Structural highlights ==~~	+	The key feature of each Immunoglobulin G is its ability to recognize and bind to one very specific epitope. This binding specificity has given antibodies a wide range of applications in both medical and research settings, such as:

-	~~This~~ is a sample ~~scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/~~2">a ~~transparent representation</scene> of the~~ protein~~. You can make your own scenes on SAT starting from scratch or loading~~ and ~~editing one of these sample scenes~~.	+	1) Identifying if a certain biomarker is present in a patient sample;
		+	2) Neutralizing a mutated protein in patients;
		+	3) Western blots, ELISAs, flow cytometry assays, and more.

-	~~</StructureSection>~~	+
-	== ~~References~~ ==	+	== Structural highlights ==
-	~~<references/>~~	+

Thomas McNamara at 22:19, 16 December 2018

Thomas McNamara — Sun, 16 Dec 2018 22:19:39 GMT

←Older revision		Revision as of 22:19, 16 December 2018
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	When a foreign pathogen invades a host organism, it is constantly coming into contact with circulating B-cells. Eventually, one particular B-cell will contain a membrane protein that recognizes and binds to a very specific region on the pathogen, called an epitope. This B-cell will then begin secreting identical Immunoglobulin G proteins whose binding sites recognize only the particular epitope. The secreted antibodies will then circulate throughout the host organism, searching for and binding to any other identical pathogens that display the same epitope. Once bound to the pathogen, the Immunoglobulin G protein can either:		When a foreign pathogen invades a host organism, it is constantly coming into contact with circulating B-cells. Eventually, one particular B-cell will contain a membrane protein that recognizes and binds to a very specific region on the pathogen, called an epitope. This B-cell will then begin secreting identical Immunoglobulin G proteins whose binding sites recognize only the particular epitope. The secreted antibodies will then circulate throughout the host organism, searching for and binding to any other identical pathogens that display the same epitope. Once bound to the pathogen, the Immunoglobulin G protein can either:
		+
		+	1) Neutralize/Immobilize the pathogen, preventing it from functioning; and/or
		+	2) Bind to immune cell receptors that facilitate pathogen degradation.
		+

	== Disease ==		== Disease ==

Thomas McNamara at 22:15, 16 December 2018

Thomas McNamara — Sun, 16 Dec 2018 22:15:24 GMT

←Older revision		Revision as of 22:15, 16 December 2018
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	Immunoglobulin G proteins, more commonly referred to as antibodies, make up a large family of secreted proteins that are potent regulators of the immune system. Furthermore, Immunoglobulin G proteins are the most common type of antibodies present in the serum, and utilize their two identical, but very unique, binding sites to recognize pathogens. It is these binding sites that differ in amino acid sequence between each Immunoglobulin G protein in a particular organism, giving each antibody a different binding target -- ultimately giving the immune system a large class of weapons that can bind to and recognize almost any foreign pathogen.		Immunoglobulin G proteins, more commonly referred to as antibodies, make up a large family of secreted proteins that are potent regulators of the immune system. Furthermore, Immunoglobulin G proteins are the most common type of antibodies present in the serum, and utilize their two identical, but very unique, binding sites to recognize pathogens. It is these binding sites that differ in amino acid sequence between each Immunoglobulin G protein in a particular organism, giving each antibody a different binding target -- ultimately giving the immune system a large class of weapons that can bind to and recognize almost any foreign pathogen.

-	This is a default text for your page '''Thomas McNamara/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs./Users/Tom/Desktop/AntibodyStrucMovie.mov
-	You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

	== Function ==		== Function ==
-	~~djdjdjdjd~~	+
		+	When a foreign pathogen invades a host organism, it is constantly coming into contact with circulating B-cells. Eventually, one particular B-cell will contain a membrane protein that recognizes and binds to a very specific region on the pathogen, called an epitope. This B-cell will then begin secreting identical Immunoglobulin G proteins whose binding sites recognize only the particular epitope. The secreted antibodies will then circulate throughout the host organism, searching for and binding to any other identical pathogens that display the same epitope. Once bound to the pathogen, the Immunoglobulin G protein can either:

	== Disease ==		== Disease ==

Thomas McNamara at 21:55, 16 December 2018

Thomas McNamara — Sun, 16 Dec 2018 21:55:50 GMT

←Older revision		Revision as of 21:55, 16 December 2018
Line 1:		Line 1:
-	==Immunoglobulin G ~~(mAB231)~~==	+	==Immunoglobulin G==

	<Structure load='1IGT' size='350' frame='true' align='right' caption='Immunoglobulin G' scene='Insert optional scene name here' />		<Structure load='1IGT' size='350' frame='true' align='right' caption='Immunoglobulin G' scene='Insert optional scene name here' />
		+
		+
		+	Immunoglobulin G proteins, more commonly referred to as antibodies, make up a large family of secreted proteins that are potent regulators of the immune system. Furthermore, Immunoglobulin G proteins are the most common type of antibodies present in the serum, and utilize their two identical, but very unique, binding sites to recognize pathogens. It is these binding sites that differ in amino acid sequence between each Immunoglobulin G protein in a particular organism, giving each antibody a different binding target -- ultimately giving the immune system a large class of weapons that can bind to and recognize almost any foreign pathogen.

	This is a default text for your page '''Thomas McNamara/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs./Users/Tom/Desktop/AntibodyStrucMovie.mov		This is a default text for your page '''Thomas McNamara/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs./Users/Tom/Desktop/AntibodyStrucMovie.mov