Molecular structure of hydrophobins studied with site-directed mutagenesis and vibrational sum-frequency generation spectroscopy

Konrad Meister, Arja Paananen, Bart Speet, Michael Lienemann, Huib Bakker

    Research output: Contribution to journalArticleScientificpeer-review

    10 Citations (Scopus)

    Abstract

    Hydrophobins are surface-active fungal proteins that adsorb to the water-air interface and self-assemble into amphiphilic, water-repelling films that have a surface elasticity that is an order of magnitude higher than other molecular films. Here we use surface-specific sum-frequency generation spectroscopy (VSFG) and site-directed mutagenesis to study the properties of class I hydrophobin (HFBI) films from Trichoderma reesei at the molecular level. We identify protein specific HFBI signals in the frequency region 1200-1700 cm-1 that have not been observed in previous VSFG studies on proteins. We find evidence that the aspartic acid residue (D30) next to the hydrophobic patch is involved in lateral intermolecular protein interactions, while the two aspartic acid residues (D40, D43) opposite to the hydrophobic patch are primarily interacting with the water solvent.
    Original languageEnglish
    Pages (from-to)9398-9402
    JournalThe Journal of Physical Chemistry B
    Volume121
    Issue number40
    DOIs
    Publication statusPublished - 12 Oct 2017
    MoE publication typeA1 Journal article-refereed

    Keywords

    • Air
    • Aspartic Acid/chemistry
    • Elasticity
    • Fungal Proteins/chemistry
    • Hydrophobic and Hydrophilic Interactions
    • Molecular Structure
    • Mutagenesis, Site-Directed
    • Spectrophotometry/methods
    • Surface Properties
    • Trichoderma
    • Vibration
    • Water/chemistry

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