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

Research output: Contribution to journalArticlepeer-review


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 (US)
Article number131101
JournalJournal of Chemical Physics
Issue number13
StatePublished - Apr 7 2019

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry


Dive into the research topics of 'Molecular structure of a hyperactive antifreeze protein adsorbed to ice'. Together they form a unique fingerprint.

Cite this