Sandbox 9876 - Revision history

Bryan Nguyen. at 19:02, 13 October 2016

Bryan Nguyen. — Thu, 13 Oct 2016 19:02:08 GMT

←Older revision		Revision as of 19:02, 13 October 2016
Line 1:		Line 1:
-	== '''Remicade (infliximab)''' ==	+	<scene name='74/744116/Test2/1'><scene name='74/744116/Bam6_tyr_141/1'>Text To Be Displayed</scene></scene>== '''Remicade (infliximab)''' ==
	<StructureSection load='4g3y_1' size='370' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='4g3y_1' size='370' side='right' caption='Caption for this structure' scene=''>

Line 6:		Line 6:
	Remicade (Infliximab) is a chimeric IgG1 monoclonal antibody consisting of 597 amino acids, weighing 149,000 Daltons. This chimeric monoclonal antibody is produced when the variable regions of a murine antibody (25%) is fused with the constant regions of a human antibody (75%) at the hinge region through a genetic engineering process. Within the hinge region, intramolecular disulfide bonds stabilize the two fragment antigen binding regions (Fab) to the fragment crystallizable region (Fc). The Fab regions are comprised of both a heavy and light chain, while the Fc region consist of only a heavy chain. Located in the folded Vh and Ch domains of the heavy chain, amino acid residues Glu-1 to Thr-226 are found. In addition, the light chains is composed of residues Asp-1 to Cys-214 that fold into the Vl and Cl domain. The heavy and light chain at the N-terminus form the variable region that functions as a receptor binding site.		Remicade (Infliximab) is a chimeric IgG1 monoclonal antibody consisting of 597 amino acids, weighing 149,000 Daltons. This chimeric monoclonal antibody is produced when the variable regions of a murine antibody (25%) is fused with the constant regions of a human antibody (75%) at the hinge region through a genetic engineering process. Within the hinge region, intramolecular disulfide bonds stabilize the two fragment antigen binding regions (Fab) to the fragment crystallizable region (Fc). The Fab regions are comprised of both a heavy and light chain, while the Fc region consist of only a heavy chain. Located in the folded Vh and Ch domains of the heavy chain, amino acid residues Glu-1 to Thr-226 are found. In addition, the light chains is composed of residues Asp-1 to Cys-214 that fold into the Vl and Cl domain. The heavy and light chain at the N-terminus form the variable region that functions as a receptor binding site.

-	After intravenously injecting Infliximab, the p55 and p75 receptors on TNF-α are neutralized when bound to the drugs high affinity receptor binding sites. The complex formed is stabilized through the vast array of weak interactions between the two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces. Specifically, TNF-α contributes to the stability by creating a hydrophobic interface through amino acid residues such as the Tyr-141 side chain. This interface is formed primarily by the C-D and E-F loop residues connecting the antiparallel 8-stranded Beta sheets. These favorable interactions are essential to the complex formed between TNF-α and infliximab Fab.	+	After intravenously injecting Infliximab, the p55 and p75 receptors on TNF-α are neutralized when bound to the drugs high affinity receptor binding sites. The complex formed is stabilized through the vast array of weak interactions between the two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces. Specifically, TNF-α contributes to the stability by creating a hydrophobic interface through amino acid residues such as the <scene name='74/744116/Bam6_tyr_141/1'>Tyr-141 side chain</scene>. This interface is formed primarily by the C-D and E-F loop residues connecting the antiparallel 8-stranded Beta sheets. These favorable interactions are essential to the complex formed between TNF-α and infliximab Fab.

	== History of Remicade ==		== History of Remicade ==

Bryan Nguyen. at 18:16, 13 October 2016

Bryan Nguyen. — Thu, 13 Oct 2016 18:16:38 GMT

←Older revision		Revision as of 18:16, 13 October 2016
Line 1:		Line 1:
-	'''Remicade (infliximab)''' ==	+	== '''Remicade (infliximab)''' ==
	<StructureSection load='4g3y_1' size='370' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='4g3y_1' size='370' side='right' caption='Caption for this structure' scene=''>
		+
		+	== Structure ==
		+
		+	Remicade (Infliximab) is a chimeric IgG1 monoclonal antibody consisting of 597 amino acids, weighing 149,000 Daltons. This chimeric monoclonal antibody is produced when the variable regions of a murine antibody (25%) is fused with the constant regions of a human antibody (75%) at the hinge region through a genetic engineering process. Within the hinge region, intramolecular disulfide bonds stabilize the two fragment antigen binding regions (Fab) to the fragment crystallizable region (Fc). The Fab regions are comprised of both a heavy and light chain, while the Fc region consist of only a heavy chain. Located in the folded Vh and Ch domains of the heavy chain, amino acid residues Glu-1 to Thr-226 are found. In addition, the light chains is composed of residues Asp-1 to Cys-214 that fold into the Vl and Cl domain. The heavy and light chain at the N-terminus form the variable region that functions as a receptor binding site.
		+
		+	After intravenously injecting Infliximab, the p55 and p75 receptors on TNF-α are neutralized when bound to the drugs high affinity receptor binding sites. The complex formed is stabilized through the vast array of weak interactions between the two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces. Specifically, TNF-α contributes to the stability by creating a hydrophobic interface through amino acid residues such as the Tyr-141 side chain. This interface is formed primarily by the C-D and E-F loop residues connecting the antiparallel 8-stranded Beta sheets. These favorable interactions are essential to the complex formed between TNF-α and infliximab Fab.

	== History of Remicade ==		== History of Remicade ==

-	Originally in search of an immunotherapy drug to combat cancer, Dr. Jan Vilcek and a team of researches made a remarkable discovery of a promising protein, tumor necrosis factor alpha. TNF-α,is a cytokine secreted by macrophages to elicit inflammation. Vilcek initially discovered the protein while studying the growth of tumors in transplantable animals, such as murine mice. It was found that this protein could not only block the growth of such tumors, but could even rid the mice completely of cancerous cells. This left many hopeful that TNF could also be employed as a therapeutic agent to fight cancers in humans.	+	Originally in search of an immunotherapy drug to combat cancer, Dr. Jan Vilcek and a team of researches made the remarkable discovery of a promising protein, tumor necrosis factor alpha. TNF-,is a cytokine secreted by macrophages to elicit inflammation. Vilcek initially discovered the protein while studying the growth of tumors in transplantable animals, such as murine mice. It was found that this protein could not only block the growth of such tumors, but could even rid the mice completely of cancerous cells. This left many hopeful that TNF could also be employed as a therapeutic agent to fight cancers in humans.
-	Beginning human trials, Vilcek and his team caught the attention of several drug companies, especially Centocor. Their hope was to have discovered a means of treating cancer using the body’s own immune system. However, within a few years of trials having been underway, this was not case. Rather, the extraordinary protein they had discovered in 1993 was highly toxic, even at low doses. Although, the study did not result in the desired outcome, the team further researched the use of TNF for other clinical applications.	+
-	Using the knowledge of TNF-as a pro-inflammatory cytokine, Vilcek started exploring the generation of antibodies for the protein. Murine mice were used as a model organism to develop the first monoclonal antibody, A2. This antibody was found to bind to TNF-thus causing the reduction of inflammation in systemic immune responses. The use of TNF inhibitors to treat diseases that were known to induce excessive inflammation, would be the foundation of Remicade. This was an engineered chimeric antibody, created by the combination of mouse and human TNF that allowed for a higher specificity and affinity to the TNF receptor. With the collaborative efforts of Centocor, Remicade became the first drug of its kind on the market.	+

-	~~== Structure ==~~	+	Beginning human trials, Vilcek and his team caught the attention of several drug companies, especially Centocor. Their hope was to have discovered a means of treating cancer using the body’s own immune system. Rather, the extraordinary protein they had discovered in 1993 was highly toxic, even at low doses. Although, the study did not result in the desired outcome, the team further researched the use of TNF for other clinical applications.

-	~~Remicade (Infliximab) is a chimeric IgG1 monoclonal antibody consisting of 597 amino acids, weighing 149,000 Daltons. A chimeric monoclonal antibody is produced when~~ the ~~variable regions~~ of a ~~murine antibody (25%) are combined with~~ the ~~constant regions~~ of ~~a human antibody (75%) at~~ the ~~hinge region~~. ~~Within~~ the ~~hinge region~~, ~~intramolecular disulfide bonds stabilize the two fragment antigen binding regions (Fab)~~ to the ~~fragment crystallizable region (Fc)~~. The ~~Fab regions are comprised~~ of ~~both a heavy and light chain~~, ~~while~~ the ~~Fc region consist~~ of ~~only a heavy chain~~. ~~Located in the folded Vh and Ch domains of the heavy chain, amino acid residues Glu-1 to Thr-226 are found. In addition~~, the ~~light chains is composed~~ of ~~residues Asp-1 to Cys-214 that fold into the Vl~~ and ~~Cl domain. The heavy and light chain at the N-terminus form the variable region~~ that ~~functions as~~ a ~~receptor binding site.~~	+	Using the knowledge of TNF-as a pro-inflammatory cytokine, Vilcek started exploring the generation of antibodies for the protein. Murine mice were used as a model organism to develop the first monoclonal antibody, A2. This antibody was found to bind to TNF-thus causing the reduction of inflammation in systemic immune responses. The use of TNF inhibitors to treat diseases that were known to induce excessive inflammation, would be the foundation of Remicade. This was an engineered chimeric antibody, created by the combination of mouse and human TNF that allowed for a higher specificity and affinity to the TNF receptor. With the collaborative efforts of Centocor, Remicade became the first receptor specific antibody for TNF- on the market.
-	~~After intravenously injecting Infliximab, the p55~~ and ~~p75 receptors on TNF-α are neutralized when bound~~ to the ~~drugs high affinity~~ receptor ~~binding sites~~. ~~The complex formed is stabilized through~~ the ~~vast array~~ of ~~weak interactions between~~ the ~~two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces. Specifically,~~ TNF-~~α contributes to~~ the stability by creating a large hydrophobic interface through its <scene name='74/744116/Tyr_141/3'>Tyr-141 side chain</scene>. This interface is formed primarily by the C-D and E-F loop residues connecting the antiparallel 8-stranded Beta sheets. Results of in vitro binding assays revealed the antibody and loops to be interacting through a molecular network.	+

	== Function ==		== Function ==

-	Upon the injection of Remicade into the body, the drug is dispersed throughout the bloodstream and to the tissues. Depending on the patient’s body surface index, the dosage of the drug administered will vary. In determining the proper amount of how much of the drug should be injected, Remicade is able to sufficiently block TNF-α from interacting with the TNF receptors (TNFR) ~~on the target cell~~, ~~thus~~ inhibiting the ~~induction~~ of IL-1 and IL-6, both of which are pro-inflammatory cytokines. When this occurs, Remicade acts as a competitive inhibitor to TNF-R. If an adequate amount is introduced, the interface will be obstructed, thus preventing TNF-α from participating further in diseases.	+	Upon the injection of Remicade into the body, the drug is dispersed throughout the bloodstream and to the tissues. Depending on the patient’s body surface index, the dosage of the drug administered will vary.
		+
		+	In determining the proper amount of how much of the drug should be injected, Remicade is able to sufficiently block TNF-α from interacting with the TNF receptors (TNFR). Thus, inhibiting the receptor from signaling production of IL-1 and IL-6, both of which are pro-inflammatory cytokines. When this occurs, Remicade acts as a competitive inhibitor to TNF-R. If an adequate amount is introduced, the interface will be obstructed, thus preventing TNF-α from participating further in diseases.
		+
	Once the complex forms, it is stabilized by the amino acid residues Gln67–His73 and Gln102–Lys112 of the C-D and E-F loops. Particularly, the weak interactions between the loops and side chains, allows for a stronger binding affinity. (ASK ABOUT ACIDIC CHAIN SUBSTITUTIONS) The strongest interaction between the two proteins is best seen in the peak region in Figure.... This arises when TNF-α is in its active form and exists as a trimer. Although, research has offered some insight into the mechanisms of how Remicade effectively inhibits TNF-α, studies have not shown a clear understanding of the extensive underlying network. Thus, more research into this matter should be pursued.		Once the complex forms, it is stabilized by the amino acid residues Gln67–His73 and Gln102–Lys112 of the C-D and E-F loops. Particularly, the weak interactions between the loops and side chains, allows for a stronger binding affinity. (ASK ABOUT ACIDIC CHAIN SUBSTITUTIONS) The strongest interaction between the two proteins is best seen in the peak region in Figure.... This arises when TNF-α is in its active form and exists as a trimer. Although, research has offered some insight into the mechanisms of how Remicade effectively inhibits TNF-α, studies have not shown a clear understanding of the extensive underlying network. Thus, more research into this matter should be pursued.

Bryan Nguyen. at 18:19, 11 October 2016

Bryan Nguyen. — Tue, 11 Oct 2016 18:19:20 GMT

←Older revision		Revision as of 18:19, 11 October 2016
Line 1:		Line 1:
-	~~<scene name='74/744116/Tyr_141/3'>Text To Be Displayed</scene>==~~ '''Remicade (infliximab)''' ==	+	'''Remicade (infliximab)''' ==
	<StructureSection load='4g3y_1' size='370' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='4g3y_1' size='370' side='right' caption='Caption for this structure' scene=''>

Bryan Nguyen. at 18:18, 11 October 2016

Bryan Nguyen. — Tue, 11 Oct 2016 18:18:42 GMT

←Older revision		Revision as of 18:18, 11 October 2016
Line 1:		Line 1:
-	== '''Remicade (infliximab)''' ==	+	<scene name='74/744116/Tyr_141/3'>Text To Be Displayed</scene>== '''Remicade (infliximab)''' ==
	<StructureSection load='4g3y_1' size='370' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='4g3y_1' size='370' side='right' caption='Caption for this structure' scene=''>

Line 11:		Line 11:

	Remicade (Infliximab) is a chimeric IgG1 monoclonal antibody consisting of 597 amino acids, weighing 149,000 Daltons. A chimeric monoclonal antibody is produced when the variable regions of a murine antibody (25%) are combined with the constant regions of a human antibody (75%) at the hinge region. Within the hinge region, intramolecular disulfide bonds stabilize the two fragment antigen binding regions (Fab) to the fragment crystallizable region (Fc). The Fab regions are comprised of both a heavy and light chain, while the Fc region consist of only a heavy chain. Located in the folded Vh and Ch domains of the heavy chain, amino acid residues Glu-1 to Thr-226 are found. In addition, the light chains is composed of residues Asp-1 to Cys-214 that fold into the Vl and Cl domain. The heavy and light chain at the N-terminus form the variable region that functions as a receptor binding site.		Remicade (Infliximab) is a chimeric IgG1 monoclonal antibody consisting of 597 amino acids, weighing 149,000 Daltons. A chimeric monoclonal antibody is produced when the variable regions of a murine antibody (25%) are combined with the constant regions of a human antibody (75%) at the hinge region. Within the hinge region, intramolecular disulfide bonds stabilize the two fragment antigen binding regions (Fab) to the fragment crystallizable region (Fc). The Fab regions are comprised of both a heavy and light chain, while the Fc region consist of only a heavy chain. Located in the folded Vh and Ch domains of the heavy chain, amino acid residues Glu-1 to Thr-226 are found. In addition, the light chains is composed of residues Asp-1 to Cys-214 that fold into the Vl and Cl domain. The heavy and light chain at the N-terminus form the variable region that functions as a receptor binding site.
-	After intravenously injecting Infliximab, the p55 and p75 receptors on TNF-α are neutralized when bound to the drugs high affinity receptor binding sites. The complex formed is stabilized through the vast array of weak interactions between the two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces. Specifically, TNF-α contributes to the stability by creating a large hydrophobic interface through its <scene name='74/744116/Tyr_141/1'>Tyr-141 side chain</scene>. This interface is formed primarily by the C-D and E-F loop residues connecting the antiparallel 8-stranded Beta sheets. Results of in vitro binding assays revealed the antibody and loops to be interacting through a molecular network.	+	After intravenously injecting Infliximab, the p55 and p75 receptors on TNF-α are neutralized when bound to the drugs high affinity receptor binding sites. The complex formed is stabilized through the vast array of weak interactions between the two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces. Specifically, TNF-α contributes to the stability by creating a large hydrophobic interface through its <scene name='74/744116/Tyr_141/3'>Tyr-141 side chain</scene>. This interface is formed primarily by the C-D and E-F loop residues connecting the antiparallel 8-stranded Beta sheets. Results of in vitro binding assays revealed the antibody and loops to be interacting through a molecular network.

	== Function ==		== Function ==

Bryan Nguyen. at 18:11, 11 October 2016

Bryan Nguyen. — Tue, 11 Oct 2016 18:11:15 GMT

←Older revision		Revision as of 18:11, 11 October 2016
Line 11:		Line 11:

	Remicade (Infliximab) is a chimeric IgG1 monoclonal antibody consisting of 597 amino acids, weighing 149,000 Daltons. A chimeric monoclonal antibody is produced when the variable regions of a murine antibody (25%) are combined with the constant regions of a human antibody (75%) at the hinge region. Within the hinge region, intramolecular disulfide bonds stabilize the two fragment antigen binding regions (Fab) to the fragment crystallizable region (Fc). The Fab regions are comprised of both a heavy and light chain, while the Fc region consist of only a heavy chain. Located in the folded Vh and Ch domains of the heavy chain, amino acid residues Glu-1 to Thr-226 are found. In addition, the light chains is composed of residues Asp-1 to Cys-214 that fold into the Vl and Cl domain. The heavy and light chain at the N-terminus form the variable region that functions as a receptor binding site.		Remicade (Infliximab) is a chimeric IgG1 monoclonal antibody consisting of 597 amino acids, weighing 149,000 Daltons. A chimeric monoclonal antibody is produced when the variable regions of a murine antibody (25%) are combined with the constant regions of a human antibody (75%) at the hinge region. Within the hinge region, intramolecular disulfide bonds stabilize the two fragment antigen binding regions (Fab) to the fragment crystallizable region (Fc). The Fab regions are comprised of both a heavy and light chain, while the Fc region consist of only a heavy chain. Located in the folded Vh and Ch domains of the heavy chain, amino acid residues Glu-1 to Thr-226 are found. In addition, the light chains is composed of residues Asp-1 to Cys-214 that fold into the Vl and Cl domain. The heavy and light chain at the N-terminus form the variable region that functions as a receptor binding site.
-	After intravenously injecting Infliximab, the p55 and p75 receptors on TNF-α are neutralized when bound to the drugs high affinity receptor binding sites. The complex formed is stabilized through the vast array of weak interactions between the two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces. Specifically, TNF-α contributes to the stability by creating a large hydrophobic interface through its Tyr-141 side chain. This interface is formed primarily by the C-D and E-F loop residues connecting the antiparallel 8-stranded Beta sheets. Results of in vitro binding assays revealed the antibody and loops to be interacting through a molecular network.	+	After intravenously injecting Infliximab, the p55 and p75 receptors on TNF-α are neutralized when bound to the drugs high affinity receptor binding sites. The complex formed is stabilized through the vast array of weak interactions between the two proteins, such as hydrogen bonds, salt bridges, and Van der Waal forces. Specifically, TNF-α contributes to the stability by creating a large hydrophobic interface through its <scene name='74/744116/Tyr_141/1'>Tyr-141 side chain</scene>. This interface is formed primarily by the C-D and E-F loop residues connecting the antiparallel 8-stranded Beta sheets. Results of in vitro binding assays revealed the antibody and loops to be interacting through a molecular network.

	== Function ==		== Function ==

Bryan Nguyen. at 20:30, 9 October 2016

Bryan Nguyen. — Sun, 09 Oct 2016 20:30:10 GMT

←Older revision		Revision as of 20:30, 9 October 2016
Line 4:		Line 4:
	== History of Remicade ==		== History of Remicade ==

-	Originally in search of an immunotherapy drug to combat cancer, Dr. Jan Vilcek and a team of researches made a remarkable discovery of a promising protein, tumor necrosis factor alpha. TNF-,is a cytokine secreted by macrophages to elicit inflammation. Vilcek initially discovered the protein while studying the growth of tumors in transplantable animals, such as murine mice. It was found that this protein could not only block the growth of such tumors, but could even rid the mice completely of cancerous cells. This left many hopeful that TNF could also be employed as a therapeutic agent to fight cancers in humans.	+	Originally in search of an immunotherapy drug to combat cancer, Dr. Jan Vilcek and a team of researches made a remarkable discovery of a promising protein, tumor necrosis factor alpha. TNF-α,is a cytokine secreted by macrophages to elicit inflammation. Vilcek initially discovered the protein while studying the growth of tumors in transplantable animals, such as murine mice. It was found that this protein could not only block the growth of such tumors, but could even rid the mice completely of cancerous cells. This left many hopeful that TNF could also be employed as a therapeutic agent to fight cancers in humans.
	Beginning human trials, Vilcek and his team caught the attention of several drug companies, especially Centocor. Their hope was to have discovered a means of treating cancer using the body’s own immune system. However, within a few years of trials having been underway, this was not case. Rather, the extraordinary protein they had discovered in 1993 was highly toxic, even at low doses. Although, the study did not result in the desired outcome, the team further researched the use of TNF for other clinical applications.		Beginning human trials, Vilcek and his team caught the attention of several drug companies, especially Centocor. Their hope was to have discovered a means of treating cancer using the body’s own immune system. However, within a few years of trials having been underway, this was not case. Rather, the extraordinary protein they had discovered in 1993 was highly toxic, even at low doses. Although, the study did not result in the desired outcome, the team further researched the use of TNF for other clinical applications.
	Using the knowledge of TNF-as a pro-inflammatory cytokine, Vilcek started exploring the generation of antibodies for the protein. Murine mice were used as a model organism to develop the first monoclonal antibody, A2. This antibody was found to bind to TNF-thus causing the reduction of inflammation in systemic immune responses. The use of TNF inhibitors to treat diseases that were known to induce excessive inflammation, would be the foundation of Remicade. This was an engineered chimeric antibody, created by the combination of mouse and human TNF that allowed for a higher specificity and affinity to the TNF receptor. With the collaborative efforts of Centocor, Remicade became the first drug of its kind on the market.		Using the knowledge of TNF-as a pro-inflammatory cytokine, Vilcek started exploring the generation of antibodies for the protein. Murine mice were used as a model organism to develop the first monoclonal antibody, A2. This antibody was found to bind to TNF-thus causing the reduction of inflammation in systemic immune responses. The use of TNF inhibitors to treat diseases that were known to induce excessive inflammation, would be the foundation of Remicade. This was an engineered chimeric antibody, created by the combination of mouse and human TNF that allowed for a higher specificity and affinity to the TNF receptor. With the collaborative efforts of Centocor, Remicade became the first drug of its kind on the market.

Bryan Nguyen. at 22:21, 8 October 2016

Bryan Nguyen. — Sat, 08 Oct 2016 22:21:32 GMT

←Older revision		Revision as of 22:21, 8 October 2016
Line 1:		Line 1:
	== '''Remicade (infliximab)''' ==		== '''Remicade (infliximab)''' ==
	<StructureSection load='4g3y_1' size='370' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='4g3y_1' size='370' side='right' caption='Caption for this structure' scene=''>
-	This is a default text for your page '''Bryan Nguyen./Remicade 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
-	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.

	== History of Remicade ==		== History of Remicade ==

Bryan Nguyen. at 16:30, 8 October 2016

Bryan Nguyen. — Sat, 08 Oct 2016 16:30:22 GMT

←Older revision		Revision as of 16:30, 8 October 2016
Line 1:		Line 1:
	== '''Remicade (infliximab)''' ==		== '''Remicade (infliximab)''' ==
-	<StructureSection load='~~4g3y.pdb~~' size='370' side='right' caption='Caption for this structure' scene=''>	+	<StructureSection load='4g3y_1' size='370' side='right' caption='Caption for this structure' scene=''>
	This is a default text for your page '''Bryan Nguyen./Remicade 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is a default text for your page '''Bryan Nguyen./Remicade 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
	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.		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.

Bryan Nguyen. at 16:18, 8 October 2016

Bryan Nguyen. — Sat, 08 Oct 2016 16:18:33 GMT

←Older revision		Revision as of 16:18, 8 October 2016
Line 1:		Line 1:
-	<Structure load='Insert PDB code or filename here' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
-
	== '''Remicade (infliximab)''' ==		== '''Remicade (infliximab)''' ==
-	<StructureSection load='4g3y.~~pdb1~~' size='370' side='right' caption='Caption for this structure' scene=''>	+	<StructureSection load='4g3y.pdb' size='370' side='right' caption='Caption for this structure' scene=''>
	This is a default text for your page '''Bryan Nguyen./Remicade 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is a default text for your page '''Bryan Nguyen./Remicade 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
	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.		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.

Bryan Nguyen. at 16:17, 8 October 2016

Bryan Nguyen. — Sat, 08 Oct 2016 16:17:35 GMT

←Older revision		Revision as of 16:17, 8 October 2016
Line 1:		Line 1:
		+	<Structure load='Insert PDB code or filename here' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
		+
	== '''Remicade (infliximab)''' ==		== '''Remicade (infliximab)''' ==
-	<StructureSection load='4g3y' size='370' side='right' caption='Caption for this structure' scene=''>	+	<StructureSection load='4g3y.pdb1' size='370' side='right' caption='Caption for this structure' scene=''>
	This is a default text for your page '''Bryan Nguyen./Remicade 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.		This is a default text for your page '''Bryan Nguyen./Remicade 1'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
	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.		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.