Year: 2012
Type: article
Abstract: Antifreeze proteins (AFPs) are specific proteins that are able to lower the freezing point of aqueous solutions relative to the melting point. Hyperactive AFPs, identified in insects, have an especially high ability to depress the freezing point by far exceeding the abilities of other AFPs. In previous studies, we postulated that the activity of AFPs can be attributed to two distinct molecular mechanisms: (i) short-range direct interaction of the protein surface with the growing ice face and (ii) long-range interaction by protein-induced water dynamics extending up to 20 Å from the protein surface. In the present paper, we combine terahertz spectroscopy and molecular simulations to prove that long-range protein-water interactions make essential contributions to the high antifreeze activity of insect AFPs from the beetle Dendroides canadensis. We also support our hypothesis by studying the effect of the addition of the osmolyte sodium citrate.
Authors: Konrad Meister, Simon Ebbinghaus, Yao Xu, John G. Duman, Arthur DeVries, Martin Gruebele, David M. Leitner, Martina Havenith
Language: English
Subfield: Physical and Theoretical Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: bronze
Awards: Protein Folding from Solution to the Living Cell, G2376503333, Antifreeze Proteins in Antarctic Fishes: Integrated Studies of Freezing Environments and Organismal Freezing Avoidance, Protein Structure-Function and Mechanism, Genes & Evolution, G503016360, Locating and controlling energy transport in proteins, clusters and nanoporous materials
OpenAlex ID: W2117957872