RiAFP: Difference between revisions

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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/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 and basal planes of ice. IBS is responsible for ordering an ice-like array of anchored “clathrate” water molecules to promote adsorption to ice (Figure 4).
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.


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[[Image:Fig7_a.jpg|frame|Fig. 5. ]]
[[Image:Fig7_a.jpg|frame|Fig. 5. Four water patterns, that could potentially independently bind the ''Ri''AFP to ice.Crystallographic waters are in red; simulation waters are in pink; dashed lines (black) represent potential hydrogen bonds]]




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'''Quiz'''
== '''Quiz''' ==
<quiz display=simple>
<quiz display=simple>


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- mealworm ''Tenebrio Molitor''
- mealworm ''Tenebrio Molitor''
+ longhorn beetle ''Rhagium inquisitor''
+ longhorn beetle ''Rhagium inquisitor''
- Antarctic bacterium ''Microdera punctipennis''
- antarctic bacterium ''Microdera punctipennis''
 
{''Ri''AFP has of the highest antifreeze activities measured for any AFP.
|type="()"}
+ true
- false
 
{ 
|type="{}"}
What is the molecular weight of ''Ri''AFP monomer?
{ 13-kDa|13 kDa }
 
{AFPs inhibit ice crystals growth through the:
|type="()"}
- adsorption inhibition model by colligative depression of the freezing point
+ adsorption inhibition model by noncolligative depression of the freezing point
- Gibbs-Thompson-Herring (i.e. Kelvin) effect by increasing the melting point of the solution
- Gibbs-Thompson-Herring (i.e. Kelvin) effect by maintaining ice front flat
 
{What is ''Ri''AFP architecture?
|type="()"}
- α domains structure
- α/β barrel
- four-helix bundle
+ β solenoid
{ 
|type="{}"}
How many β sheets do ''Ri''AFP have?
{ 13 }
 
{What residues are crucial for maintaining antifreeze activity?
|type="()"}
+ Threonine
- Alanine
- Serine
- Glutamine
- Isoleucine
 
{''Ri''AFP has two disulfide bonds.
|type="()"}
- true
+ false
 
{''Ri''AFP binds ice crystals:
|type="()"}
- covalently
+ via anchored “clathrate” water molecules
- directly
- through van der Waals' interactions
 
</StructureSection>
</StructureSection>
==3D structures of antifreeze protein==
==3D structures of antifreeze protein==
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== References ==
== References ==
<references/>
<references/>
[[Category:Pages with quizzes]]
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