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 tidsskriftTidsskriftartikelForskningpeer review

Resumé

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.
OriginalsprogEngelsk
Artikelnummer131101
TidsskriftThe Journal of Chemical Physics
Vol/bind150
Udgave nummer13
Antal sider4
ISSN0021-9606
DOI
StatusUdgivet - 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 rucforsk@ruc.dk

Emneord

  • Antifryseprotein
  • struktur
  • Is

Citer dette

Meister, K., Moll, C. J., Chakraborty, S., Jana, B., DeVries, A., Ramløv, H., & Bakker, H. J. (2019). Molecular structure of a hyperactive antifreeze protein adsorbed to ice. The Journal of Chemical Physics, 150(13), [131101]. https://doi.org/10.1063/1.5090589
Meister, Konrad ; Moll, C.J. ; Chakraborty, S. ; Jana, B. ; DeVries, Arthur ; Ramløv, Hans ; Bakker, H.J. / Molecular structure of a hyperactive antifreeze protein adsorbed to ice. I: The Journal of Chemical Physics. 2019 ; Bind 150, Nr. 13.
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Meister, K, Moll, CJ, Chakraborty, S, Jana, B, DeVries, A, Ramløv, H & Bakker, HJ 2019, 'Molecular structure of a hyperactive antifreeze protein adsorbed to ice' The Journal of Chemical Physics, bind 150, nr. 13, 131101. https://doi.org/10.1063/1.5090589

Molecular structure of a hyperactive antifreeze protein adsorbed to ice. / Meister, Konrad ; Moll, C.J.; Chakraborty, S.; Jana, B.; DeVries, Arthur; Ramløv, Hans; Bakker, H.J.

I: The Journal of Chemical Physics, Bind 150, Nr. 13, 131101, 04.2019.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Molecular structure of a hyperactive antifreeze protein adsorbed to ice

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 rucforsk@ruc.dk

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 - struktur

KW - Is

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