Observation of pH-Induced Protein Reorientation at the Water Surface

Konrad Meister (Corresponding Author), Steven J. Roeter, Arja Paananen, Sander Woutersen, Jan Versluis, Géza R. Szilvay, Huib J. Bakker

    Research output: Contribution to journalArticleScientificpeer-review

    19 Citations (Scopus)


    Hydrophobins are surface-active proteins that form a hydrophobic, water-repelling film around aerial fungal structures. They have a compact, particle-like structure, in which hydrophilic and hydrophobic regions are spatially separated. This surface property renders them amphiphilic and is reminiscent of synthetic Janus particles. Here we report surface-specific chiral and nonchiral vibrational sum-frequency generation spectroscopy (VSFG) measurements of hydrophobins adsorbed to their natural place of action, the air-water interface. We observe that hydrophobin molecules undergo a reversible change in orientation (tilt) at the interface when the pH is varied. We explain this local orientation toggle from the modification of the interprotein interactions and the interaction of hydrophobin with the water solvent, following the pH-induced change of the charge state of particular amino acids.
    Original languageEnglish
    Pages (from-to)1772-1776
    JournalThe Journal of Physical Chemistry Letters
    Issue number8
    Publication statusPublished - 20 Apr 2017
    MoE publication typeA1 Journal article-refereed


    • hydophobin
    • HFBII
    • air-water interface
    • interfacial behavior
    • vibrational sum-frequency generation spectroscopy
    • VSFGS
    • Water
    • Protein Structure, Secondary
    • Air
    • Adsorption
    • Fungal Proteins/chemistry
    • Hydrophobic and Hydrophilic Interactions
    • Protein Conformation


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