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Interfacial water controls the process of adsorption of hyperactive antifreeze proteins onto the ice surface
Abstrakt
A mechanism of interactions between the ice-binding surface of a hyperactive antifreeze protein molecule and the ice surface is proposed, involving the influence of water present between the two surfaces on the behavior of the approaching molecule. It is demonstrated that the interfacial water, even before its full solidification, can act as a factor that pushes away or pulls nearer the protein molecule to ensure its proper positioning. It is possible thanks to the structural properties of interfacial water. These properties include the ability to create high-volume aggregates of water molecules. They can appear near and be anchored to both the ice-binding plane of the anti- freeze molecule and the ice surface. When an AFP approaches the growing face of ice, these high-volume, ordered structures near the ice and near the AFP molecule merge together smoothly, but only if the proper distance be- tween the ice and the AFP is ensured. If this is not the case, the resulting merged structure is deformed from its preferred shape and as a result a force occurs that attempts to correct the positioning of the protein. Only then the crystallization of the merged aggregate can proceed unhampered which results in binding of the AFP molecule onto the ice.
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- Wersja publikacji
- Accepted albo Published Version
- DOI:
- Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.1016/j.molliq.2020.112909
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Informacje szczegółowe
- Kategoria:
- Publikacja w czasopiśmie
- Typ:
- artykuły w czasopismach
- Opublikowano w:
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JOURNAL OF MOLECULAR LIQUIDS
nr 306,
ISSN: 0167-7322 - Język:
- angielski
- Rok wydania:
- 2020
- Opis bibliograficzny:
- Grabowska J., Kuffel A., Zielkiewicz J.: Interfacial water controls the process of adsorption of hyperactive antifreeze proteins onto the ice surface// JOURNAL OF MOLECULAR LIQUIDS -Vol. 306, (2020), s.112909-
- DOI:
- Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.1016/j.molliq.2020.112909
- Weryfikacja:
- Politechnika Gdańska
wyświetlono 72 razy