RiAFP - Revision history

Angel Herraez: adding pages to the "Pages with quizzes" category

2018-01-24T17:46:30Z

adding pages to the "Pages with quizzes" category

← Older revision		Revision as of 17:46, 24 January 2018
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	== References ==		== References ==
	<references/>		<references/>

			[[Category:Pages with quizzes]]

Vera Sirotinskaya at 08:08, 26 January 2015

2015-01-26T08:08:06Z

← Older revision		Revision as of 08:08, 26 January 2015
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	== Molecular Basis for Ice Binding ==		== Molecular Basis for Ice Binding ==
	IBS is less hydrophilic than the other β–sheet, which is consistent with its role of interacting with the ice (Figure 3). Adsorption of the AFP ice-binding surface to ice is facilitated by the flatness of the IBS of the ''Ri''AFP. The Sc (shape complementarity) values between ''Ri''AFP and ice interfaces range from 0.75-0.78, where 1.0 indicates perfect match. For comparison, antigen-antibody complexes usually have their Sc values in the range of 0.64–0.68.		IBS is less hydrophilic than the other β–sheet, which is consistent with its role of interacting with the ice (Figure 3). Adsorption of the AFP ice-binding surface to ice is facilitated by the flatness of the IBS of the ''Ri''AFP. The Sc (shape complementarity) values between ''Ri''AFP and ice interfaces range from 0.75-0.78, where 1.0 indicates perfect match. For comparison, antigen-antibody complexes usually have their Sc values in the range of 0.64–0.68.
	Thr hydroxyls bind 3 ranks of 6 <scene name='60/607864/Isosurface/5'>water molecules</scene> with equivalent spacing between the 4 ranks of Thr side chains. These water molecules are bound tightly, they have lost both translational and rotational freedom and resemble those in an ice lattice. The waters observed in the computational simulation appear to be organized in an ice-like formation, with close matches to the primary prism (Figure 4) and basal planes of ice. IBS is responsible for ordering an ice-like array of anchored “clathrate” water molecules to promote adsorption to ice.		Thr hydroxyls bind 3 ranks of 6 <scene name='60/607864/Isosurface/6'>water molecules</scene> with equivalent spacing between the 4 ranks of Thr side chains. These water molecules are bound tightly, they have lost both translational and rotational freedom and resemble those in an ice lattice. The waters observed in the computational simulation appear to be organized in an ice-like formation, with close matches to the primary prism (Figure 4) and basal planes of ice. IBS is responsible for ordering an ice-like array of anchored “clathrate” water molecules to promote adsorption to ice.

	{\|style="margin: 0 auto;"		{\|style="margin: 0 auto;"

Vera Sirotinskaya at 08:05, 26 January 2015

2015-01-26T08:05:49Z

← Older revision		Revision as of 08:05, 26 January 2015
Line 25:		Line 25:
	== Molecular Basis for Ice Binding ==		== Molecular Basis for Ice Binding ==
	IBS is less hydrophilic than the other β–sheet, which is consistent with its role of interacting with the ice (Figure 3). Adsorption of the AFP ice-binding surface to ice is facilitated by the flatness of the IBS of the ''Ri''AFP. The Sc (shape complementarity) values between ''Ri''AFP and ice interfaces range from 0.75-0.78, where 1.0 indicates perfect match. For comparison, antigen-antibody complexes usually have their Sc values in the range of 0.64–0.68.		IBS is less hydrophilic than the other β–sheet, which is consistent with its role of interacting with the ice (Figure 3). Adsorption of the AFP ice-binding surface to ice is facilitated by the flatness of the IBS of the ''Ri''AFP. The Sc (shape complementarity) values between ''Ri''AFP and ice interfaces range from 0.75-0.78, where 1.0 indicates perfect match. For comparison, antigen-antibody complexes usually have their Sc values in the range of 0.64–0.68.
	Thr hydroxyls bind 3 ranks of 6 <scene name='60/607864/Isosurface/4'>water molecules</scene> with equivalent spacing between the 4 ranks of Thr side chains. These water molecules are bound tightly, they have lost both translational and rotational freedom and resemble those in an ice lattice. The waters observed in the computational simulation appear to be organized in an ice-like formation, with close matches to the primary prism (Figure 4) and basal planes of ice. IBS is responsible for ordering an ice-like array of anchored “clathrate” water molecules to promote adsorption to ice.		Thr hydroxyls bind 3 ranks of 6 <scene name='60/607864/Isosurface/5'>water molecules</scene> with equivalent spacing between the 4 ranks of Thr side chains. These water molecules are bound tightly, they have lost both translational and rotational freedom and resemble those in an ice lattice. The waters observed in the computational simulation appear to be organized in an ice-like formation, with close matches to the primary prism (Figure 4) and basal planes of ice. IBS is responsible for ordering an ice-like array of anchored “clathrate” water molecules to promote adsorption to ice.

	{\|style="margin: 0 auto;"		{\|style="margin: 0 auto;"

Vera Sirotinskaya at 08:04, 26 January 2015

2015-01-26T08:04:32Z

← Older revision		Revision as of 08:04, 26 January 2015
Line 25:		Line 25:
	== Molecular Basis for Ice Binding ==		== Molecular Basis for Ice Binding ==
	IBS is less hydrophilic than the other β–sheet, which is consistent with its role of interacting with the ice (Figure 3). Adsorption of the AFP ice-binding surface to ice is facilitated by the flatness of the IBS of the ''Ri''AFP. The Sc (shape complementarity) values between ''Ri''AFP and ice interfaces range from 0.75-0.78, where 1.0 indicates perfect match. For comparison, antigen-antibody complexes usually have their Sc values in the range of 0.64–0.68.		IBS is less hydrophilic than the other β–sheet, which is consistent with its role of interacting with the ice (Figure 3). Adsorption of the AFP ice-binding surface to ice is facilitated by the flatness of the IBS of the ''Ri''AFP. The Sc (shape complementarity) values between ''Ri''AFP and ice interfaces range from 0.75-0.78, where 1.0 indicates perfect match. For comparison, antigen-antibody complexes usually have their Sc values in the range of 0.64–0.68.
	Thr hydroxyls bind 3 ranks of 6 <scene name='60/607864/Isosurface/3'>water molecules</scene> with equivalent spacing between the 4 ranks of Thr side chains. These water molecules are bound tightly, they have lost both translational and rotational freedom and resemble those in an ice lattice. The waters observed in the computational simulation appear to be organized in an ice-like formation, with close matches to the primary prism (Figure 4) and basal planes of ice. IBS is responsible for ordering an ice-like array of anchored “clathrate” water molecules to promote adsorption to ice.		Thr hydroxyls bind 3 ranks of 6 <scene name='60/607864/Isosurface/4'>water molecules</scene> with equivalent spacing between the 4 ranks of Thr side chains. These water molecules are bound tightly, they have lost both translational and rotational freedom and resemble those in an ice lattice. The waters observed in the computational simulation appear to be organized in an ice-like formation, with close matches to the primary prism (Figure 4) and basal planes of ice. IBS is responsible for ordering an ice-like array of anchored “clathrate” water molecules to promote adsorption to ice.

	{\|style="margin: 0 auto;"		{\|style="margin: 0 auto;"

Vera Sirotinskaya: Undo revision 2368239 by Vera Sirotinskaya (Talk)

2015-01-26T07:26:42Z

Undo revision 2368239 by Vera Sirotinskaya (Talk)

← Older revision		Revision as of 07:26, 26 January 2015
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	~~</StructureSection>~~
	~~==3D structures of antifreeze protein==~~
	~~[[Antifreeze protein]]~~

	== '''Quiz''' ==		== '''Quiz''' ==
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	- directly		- directly
	- through van der Waals' interactions		- through van der Waals' interactions

			</StructureSection>
			==3D structures of antifreeze protein==
			[[Antifreeze protein]]

	== References ==		== References ==
	<references/>		<references/>

Vera Sirotinskaya at 07:25, 26 January 2015

2015-01-26T07:25:38Z

← Older revision		Revision as of 07:25, 26 January 2015
Line 57:		Line 57:





			</StructureSection>
			==3D structures of antifreeze protein==
			[[Antifreeze protein]]

	== '''Quiz''' ==		== '''Quiz''' ==
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	- directly		- directly
	- through van der Waals' interactions		- through van der Waals' interactions

	~~</StructureSection>~~
	~~==3D structures of antifreeze protein==~~
	~~[[Antifreeze protein]]~~

	== References ==		== References ==
	<references/>		<references/>

Vera Sirotinskaya at 07:17, 26 January 2015

2015-01-26T07:17:52Z

← Older revision		Revision as of 07:17, 26 January 2015
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	+ false		+ false

			{''Ri''AFP binds ice crystals:
			\|type="()"}
			- covalently
			+ via anchored “clathrate” water molecules
			- directly
			- through van der Waals' interactions

	</StructureSection>		</StructureSection>

Vera Sirotinskaya at 07:07, 26 January 2015

2015-01-26T07:07:35Z

← Older revision		Revision as of 07:07, 26 January 2015
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	- Glutamine		- Glutamine
	- Isoleucine		- Isoleucine

			{''Ri''AFP has two disulfide bonds.
			\|type="()"}
			- true
			+ false


	</StructureSection>		</StructureSection>

Vera Sirotinskaya at 07:03, 26 January 2015

2015-01-26T07:03:29Z

← Older revision		Revision as of 07:03, 26 January 2015
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	How many β sheets do ''Ri''AFP have?		How many β sheets do ''Ri''AFP have?
	{ 13 }		{ 13 }

			{What residues are crucial for maintaining antifreeze activity?
			\|type="()"}
			+ Threonine
			- Alanine
			- Serine
			- Glutamine
			- Isoleucine

	</StructureSection>		</StructureSection>

Vera Sirotinskaya at 06:59, 26 January 2015

2015-01-26T06:59:08Z

← Older revision		Revision as of 06:59, 26 January 2015
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	+ β solenoid		+ β solenoid

			{
			\|type="{}"}
			How many β sheets do ''Ri''AFP have?
			{ 13 }

	</StructureSection>		</StructureSection>