Molecular structure of a hyperactive antifreeze protein adsorbed to ice

K. Meister; C. J. Moll; S. Chakraborty; B. Jana; A. L. DeVries; H. Ramløv; H. J. Bakker

doi:10.1063/1.5090589

Molecular structure of a hyperactive antifreeze protein adsorbed to ice

K. Meister, C. J. Moll, S. Chakraborty, B. Jana, A. L. DeVries, H. Ramløv, H. J. Bakker

Evolution, Ecology, and Behavior

Research output: Contribution to journal › Article › 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.

Original language	English (US)
Article number	131101
Journal	Journal of Chemical Physics
Volume	150
Issue number	13
DOIs	https://doi.org/10.1063/1.5090589
State	Published - Apr 7 2019

ASJC Scopus subject areas

Physics and Astronomy(all)
Physical and Theoretical Chemistry

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10.1063/1.5090589

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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.",

author = "K. Meister and Moll, {C. J.} and S. Chakraborty and B. Jana and DeVries, {A. L.} and H. Raml{\o}v and Bakker, {H. J.}",

note = "Funding Information: This work was part of the research program of the Netherlands Organization for Scientific Research (NWO) and was performed at the research institute AMOLF. B.J. acknowledges financial support from the Department of Science and Technology (India) SERB (Grant No. EMR/2016/001333). The authors acknowledge the central supercomputing facility (CRAY) at Indian Association for the Cultivation of Science, Kolkata, India. Publisher Copyright: {\textcopyright} 2019 Author(s).",

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AU - Meister, K.

AU - Moll, C. J.

AU - Chakraborty, S.

AU - Jana, B.

AU - DeVries, A. L.

AU - Ramløv, H.

AU - Bakker, H. J.

N1 - Funding Information: This work was part of the research program of the Netherlands Organization for Scientific Research (NWO) and was performed at the research institute AMOLF. B.J. acknowledges financial support from the Department of Science and Technology (India) SERB (Grant No. EMR/2016/001333). The authors acknowledge the central supercomputing facility (CRAY) at Indian Association for the Cultivation of Science, Kolkata, India. Publisher Copyright: © 2019 Author(s).

PY - 2019/4/7

Y1 - 2019/4/7

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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Molecular structure of a hyperactive antifreeze protein adsorbed to ice

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