Thermal hysteresis protein YL-1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
<Structure load='1ezg' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<Structure load='1ezg' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
-
[[Image:IceBind 4.png |thumb|400px| The ice formation of water (red spheres) being scrambled (blue spheres) by the protein]]
+
[[Image:IceBind 4.png |thumb|400px| The beta sheet roll motif lines up the amino acid chain such that each turn interacts with a unit cell of the water ice crystal]]

Revision as of 02:44, 1 May 2025

Insert caption here

Drag the structure with the mouse to rotate
The beta sheet roll motif lines up the amino acid chain such that each turn interacts with a unit cell of the water ice crystal
The beta sheet roll motif lines up the amino acid chain such that each turn interacts with a unit cell of the water ice crystal


Tenebrio molitor (Yellow mealworm beetle)

Contributes to protect body fluid from freezing at subzero temperatures. Lowers the freezing point of the hemolymph by about 2.5 degrees at a concentration of 1 mg/ml. Binds to nascent ice crystals and prevents further growth

Structural highlights


References

Liou YC, Tocilj A, Davies PL, Jia Z. Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein. Nature. 2000 Jul 20;406(6793):322-4. doi: 10.1038/35018604. PMID: 10917536.

Proteopedia Page Contributors and Editors (what is this?)

Justin Paluba

Retrieved from "http://52.214.119.220/wiki/index.php/Thermal_hysteresis_protein_YL-1"
Personal tools