Interaction of antifreeze proteins with water

Ilja Karina Voets, Konrad Meister

    Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

    Abstract

    Antifreeze proteins and antifreeze glycoproteins (AF(G)Ps) enable the survival of various cold-adapted organisms in freezing and subfreezing habitats by preventing the macroscopic growth of ice crystals. Regardless of their great structural diversity are all AF(G)Ps capable to adhere to growing ice crystals, a quality that is essential for their biological functions. Despite commercial interest and significant scientific breakthroughs has the precise working mechanism of antifreeze proteins not yet been unraveled. In this chapter we highlight the latest state-of-the art experimental and theoretical antifreeze protein research on the solution behavior of AF(G)Ps and their interaction with the solvent. Protein-water interactions are of general interest owing to the importance of protein hydration for the structure, stability, and activity of almost all proteins. We focus in particular on the direct interaction of AF(G)Ps with water and its role in the working mechanism of these unique proteins.

    Original languageEnglish
    Title of host publicationAntifreeze Proteins Volume 2
    Subtitle of host publicationBiochemistry, Molecular Biology and Applications
    PublisherSpringer
    Pages109-127
    Number of pages19
    ISBN (Electronic)9783030419486
    ISBN (Print)9783030419479
    DOIs
    Publication statusPublished - 1 Jan 2020

    Keywords

    • Antifreeze proteins
    • Hydration shell
    • Ice-binding site
    • Non-colligative freezing point depression
    • Protein-water interactions

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