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

Chemistry Department

AMOLF
Indian Association for the Cultivation of Science
University of Illinois at Urbana-Champaign
Roskilde University

Research output: Contribution to journal › Article › peer-review

39 Scopus citations

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

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

AU - Meister, K.

AU - Moll, C. J.

AU - Chakraborty, S.

AU - Jana, B.

AU - DeVries, A. L.

AU - Ramløv, H.

AU - Bakker, H. J.

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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DO - 10.1063/1.5090589

M3 - Article

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VL - 150

JO - Journal of Chemical Physics

JF - Journal of Chemical Physics

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ER -

Molecular structure of a hyperactive antifreeze protein adsorbed to ice

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