Sandbox Reserved 1392 - Revision history

Student at 03:15, 1 March 2018

Student — Thu, 01 Mar 2018 03:15:52 GMT

←Older revision		Revision as of 03:15, 1 March 2018
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	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.) <scene name='77/777712/Beta-sheets/1'>Beta sheets</scene>		The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.) <scene name='77/777712/Beta-sheets/1'>Beta sheets</scene>

-	The helix region of the E-cadherin molecule prevents the abnormal regulation of the junction complex, thus ensuring complete and correct translation of the spliced mRNA into protein.	+	The helix region of the E-cadherin molecule prevents the abnormal regulation of the junction complex, thus ensuring complete and correct translation of the spliced mRNA into protein. <scene name='77/777712/Helix_region/1'>Helix Region</scene>
-	<scene name='77/777712/Helix_region/1'>Helix Region</scene>	+
	== References ==		== References ==
	<references/>		<references/>

Student at 03:12, 1 March 2018

Student — Thu, 01 Mar 2018 03:12:38 GMT

←Older revision		Revision as of 03:12, 1 March 2018
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	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.) <scene name='77/777712/Beta-sheets/1'>Beta sheets</scene>		The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.) <scene name='77/777712/Beta-sheets/1'>Beta sheets</scene>

		+	The helix region of the E-cadherin molecule prevents the abnormal regulation of the junction complex, thus ensuring complete and correct translation of the spliced mRNA into protein.
	<scene name='77/777712/Helix_region/1'>Helix Region</scene>		<scene name='77/777712/Helix_region/1'>Helix Region</scene>
	== References ==		== References ==

Student at 03:07, 1 March 2018

Student — Thu, 01 Mar 2018 03:07:01 GMT

←Older revision		Revision as of 03:07, 1 March 2018
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	<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>		<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>
-	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.) <scene name='77/777712/Beta-~~sheets_of_e-cadherin~~/1'>Beta ~~strand of E-cadherin~~</scene>	+	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.) <scene name='77/777712/Beta-sheets/1'>Beta sheets</scene>

	<scene name='77/777712/Helix_region/1'>Helix Region</scene>		<scene name='77/777712/Helix_region/1'>Helix Region</scene>

Student at 03:01, 1 March 2018

Student — Thu, 01 Mar 2018 03:01:46 GMT

←Older revision		Revision as of 03:01, 1 March 2018
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	<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>		<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>
-	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.) <scene name='77/777712/Beta-sheets_of_e-cadherin/1'>Beta strand of E-cadherin	+	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.) <scene name='77/777712/Beta-sheets_of_e-cadherin/1'>Beta strand of E-cadherin</scene>
-	</scene>	+
	<scene name='77/777712/Helix_region/1'>Helix Region</scene>		<scene name='77/777712/Helix_region/1'>Helix Region</scene>
	== References ==		== References ==

Student at 03:00, 1 March 2018

Student — Thu, 01 Mar 2018 03:00:38 GMT

←Older revision		Revision as of 03:00, 1 March 2018
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	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.) <scene name='77/777712/Beta-sheets_of_e-cadherin/1'>Beta strand of E-cadherin		The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.) <scene name='77/777712/Beta-sheets_of_e-cadherin/1'>Beta strand of E-cadherin
	</scene>		</scene>
		+	<scene name='77/777712/Helix_region/1'>Helix Region</scene>
	== References ==		== References ==
	<references/>		<references/>

Student at 02:55, 1 March 2018

Student — Thu, 01 Mar 2018 02:55:55 GMT

←Older revision		Revision as of 02:55, 1 March 2018
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	<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>		<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>
-	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states. <scene name='77/777712/Beta-sheets_of_e-cadherin/1'>Beta strand of E-cadherin	+	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.) <scene name='77/777712/Beta-sheets_of_e-cadherin/1'>Beta strand of E-cadherin
	</scene>		</scene>
	== References ==		== References ==

Student at 02:54, 1 March 2018

Student — Thu, 01 Mar 2018 02:54:12 GMT

←Older revision		Revision as of 02:54, 1 March 2018
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	<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>		<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>
-	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. <scene name='77/777712/Beta-sheets_of_e-cadherin/1'>Beta strand of E-cadherin	+	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states. <scene name='77/777712/Beta-sheets_of_e-cadherin/1'>Beta strand of E-cadherin
	</scene>		</scene>
	== References ==		== References ==

Student at 02:51, 1 March 2018

Student — Thu, 01 Mar 2018 02:51:27 GMT

←Older revision		Revision as of 02:51, 1 March 2018
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	<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>		<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>
-	<scene name='77/777712/Beta-~~strands_of_e~~-cadherin/1'>Beta strand of E-cadherin	+	The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. <scene name='77/777712/Beta-sheets_of_e-cadherin/1'>Beta strand of E-cadherin
	</scene>		</scene>
	== References ==		== References ==

Student at 02:46, 1 March 2018

Student — Thu, 01 Mar 2018 02:46:54 GMT

←Older revision		Revision as of 02:46, 1 March 2018
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	==Human E-cadherin Protein==		==Human E-cadherin Protein==
	<StructureSection load='2o72' size='340' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='2o72' size='340' side='right' caption='Caption for this structure' scene=''>
-	This is a default text for your page ''''''. 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.

	== Function ==		== Function ==
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	<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>		<scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene>
-		+	<scene name='77/777712/Beta-strands_of_e-cadherin/1'>Beta strand of E-cadherin
		+	</scene>
	== References ==		== References ==
	<references/>		<references/>

Student at 02:44, 1 March 2018

Student — Thu, 01 Mar 2018 02:44:20 GMT

←Older revision		Revision as of 02:44, 1 March 2018
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	==Human E-cadherin Protein==		==Human E-cadherin Protein==
	<StructureSection load='2o72' size='340' side='right' caption='Caption for this structure' scene=''>		<StructureSection load='2o72' size='340' side='right' caption='Caption for this structure' scene=''>
		+	This is a default text for your page ''''''. 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.

	== Function ==		== Function ==