Molecular structure of a hyperactive antifreeze protein adsorbed to ice

Konrad  Meister; C.J. Moll; S. Chakraborty; B. Jana; Arthur DeVries; Hans Ramløv; H.J. Bakker

doi:10.1063/1.5090589

Molecular structure of a hyperactive antifreeze protein adsorbed to ice

Konrad Meister, C.J. Moll, S. Chakraborty, B. Jana, Arthur DeVries, Hans Ramløv, H.J. Bakker

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Abstract

Antifreeze proteins (AFPs) are a unique class of proteins that bind to ice crystal surfaces and arrest their growth. The working mechanism of AFPs is not well understood because, as of yet, it was not possible to perform molecular-scale studies of AFPs adsorbed to the surface of ice. Here, we study the structural properties of an AFP from the insect Rhagium mordax (RmAFP) adsorbed to ice with surface specific heterodyne-detected vibrational sum-frequency generation spectroscopy and molecular dynamic simulations. We find that RmAFP, unlike other proteins, retains its hydrating water molecules upon adsorption to the ice surface. This hydration water has an orientation and hydrogen-bond structure different from the ice surface, thereby inhibiting the insertion of water layers in between the protein and the ice surface.

Originalsprog	Engelsk
Artikelnummer	131101
Tidsskrift	The Journal of Chemical Physics
Vol/bind	150
Udgave nummer	13
Antal sider	4
ISSN	0021-9606
DOI	https://doi.org/10.1063/1.5090589
Status	Udgivet - apr. 2019

Bibliografisk note

This article has been found as a 'Free version' from the Publisher on XXX 2019. If access to the article closes, please notify [email protected]

Emneord

Antifryseprotein
struktur
Is

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10.1063/1.5090589

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3 Tidsskriftartikel

Detecting seasonal variation of antifreeze protein distribution in Rhagium mordax using immunofluorescence and high resolution microscopy
Buch, J. L. & Ramløv, H., 2017, I: Cryobiology. 74, s. 132-140 9 s.
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Åben adgang
Fil
Low thermodynamic but high kinetic stability of an antifreeze protein from Rhagium mordax
Friis, D. S., Johnsen, J. L., Kristiansen, E., Westh, P. & Ramløv, H., jun. 2014, I: Protein Science. 23, 6, s. 760-768 9 s.
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review
Hyperactive antifreeze proteins from longhorn beetles: Some structural insights
Kristiansen, E., Wilkens, C., Vincents, B., Friis, D. S., Lorentzen, A. B., Jenssen, H., Løbner-Olesen, A. & Ramløv, H., 2012, I: Journal of Insect Physiology. 58, 11, s. 1502-1510 9 s.
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Citer dette

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title = "Molecular structure of a hyperactive antifreeze protein adsorbed to ice",

abstract = "Antifreeze proteins (AFPs) are a unique class of proteins that bind to ice crystal surfaces and arrest their growth. The working mechanism of AFPs is not well understood because, as of yet, it was not possible to perform molecular-scale studies of AFPs adsorbed to the surface of ice. Here, we study the structural properties of an AFP from the insect Rhagium mordax (RmAFP) adsorbed to ice with surface specific heterodyne-detected vibrational sum-frequency generation spectroscopy and molecular dynamic simulations. We find that RmAFP, unlike other proteins, retains its hydrating water molecules upon adsorption to the ice surface. This hydration water has an orientation and hydrogen-bond structure different from the ice surface, thereby inhibiting the insertion of water layers in between the protein and the ice surface.",

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note = "This article has been found as a 'Free version' from the Publisher on XXX 2019. If access to the article closes, please notify [email protected]",

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AU - Meister, Konrad

AU - Moll, C.J.

AU - Chakraborty, S.

AU - Jana, B.

AU - DeVries, Arthur

AU - Ramløv, Hans

AU - Bakker, H.J.

N1 - This article has been found as a 'Free version' from the Publisher on XXX 2019. If access to the article closes, please notify [email protected]

PY - 2019/4

Y1 - 2019/4

N2 - Antifreeze proteins (AFPs) are a unique class of proteins that bind to ice crystal surfaces and arrest their growth. The working mechanism of AFPs is not well understood because, as of yet, it was not possible to perform molecular-scale studies of AFPs adsorbed to the surface of ice. Here, we study the structural properties of an AFP from the insect Rhagium mordax (RmAFP) adsorbed to ice with surface specific heterodyne-detected vibrational sum-frequency generation spectroscopy and molecular dynamic simulations. We find that RmAFP, unlike other proteins, retains its hydrating water molecules upon adsorption to the ice surface. This hydration water has an orientation and hydrogen-bond structure different from the ice surface, thereby inhibiting the insertion of water layers in between the protein and the ice surface.

AB - Antifreeze proteins (AFPs) are a unique class of proteins that bind to ice crystal surfaces and arrest their growth. The working mechanism of AFPs is not well understood because, as of yet, it was not possible to perform molecular-scale studies of AFPs adsorbed to the surface of ice. Here, we study the structural properties of an AFP from the insect Rhagium mordax (RmAFP) adsorbed to ice with surface specific heterodyne-detected vibrational sum-frequency generation spectroscopy and molecular dynamic simulations. We find that RmAFP, unlike other proteins, retains its hydrating water molecules upon adsorption to the ice surface. This hydration water has an orientation and hydrogen-bond structure different from the ice surface, thereby inhibiting the insertion of water layers in between the protein and the ice surface.

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KW - Is

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JF - The Journal of Chemical Physics

IS - 13

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ER -

Molecular structure of a hyperactive antifreeze protein adsorbed to ice

Abstract

Bibliografisk note

Emneord

Link til dokument

Andre filer og links

Publikation

Detecting seasonal variation of antifreeze protein distribution in Rhagium mordax using immunofluorescence and high resolution microscopy

Low thermodynamic but high kinetic stability of an antifreeze protein from Rhagium mordax

Hyperactive antifreeze proteins from longhorn beetles: Some structural insights

Citer dette