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

Research output: Contribution to journalJournal articleResearchpeer-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 languageEnglish
Article number131101
JournalThe Journal of Chemical Physics
Volume150
Issue number13
Number of pages4
ISSN0021-9606
DOIs
Publication statusPublished - Apr 2019

Bibliographical note

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