Thermal hysteresis protein YL-1
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<scene name='10/1080036/Ice-binding_site/1'>Ice-binding</scene> | <scene name='10/1080036/Ice-binding_site/1'>Ice-binding</scene> | ||
- | + | <scene name='10/1080036/Cysteine_sulfur_bridges/1'>Cysteine sulfur bridges</scene> | |
== References == | == References == | ||
<references/> | <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. | 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. |
Revision as of 03:09, 1 May 2025
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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.