Self-assembled films of hydrophobin protein HFBIII from Trichoderma reesei

Kaisa Kisko*, Géza R. Szilvay, Elina Vuorimaa, Helge Lemmetyinen, Markus B. Linder, Mika Torkkeli, Ritva Serimaa

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

16 Citations (Scopus)


Hydrophobins are a group of small amphiphilic proteins which are known to self-assemble on interfaces. They contain eight conserved cysteine residues, which make four disulfide bridges. A new hydrophobin protein, HFBIII, from the fungus Trichoderma reesei contains one extra cysteine residue, giving the protein a naturally reactive site. The self-assembly of hydrophobin protein HFBIII was studied using grazing-incidence X-ray diffraction and reflectivity. HFBIII self-assembles into a hexagonally ordered monolayer at an air/water interface and also forms crystalline coatings on a silicon substrate. The lattice constants for the hexagonal coatings are a = b = 56.5 Å, γ = 120°. The self-assembled structure in the HFBIII film is very similar to those formed by two other T. reesei hydrophobins, HFBI and HFBII.

Original languageEnglish
Pages (from-to)355-360
Number of pages6
JournalJournal of Applied Crystallography
Publication statusPublished - Apr 2007
MoE publication typeA1 Journal article-refereed


  • Grazing-incidence X-ray diffraction
  • Hydrophobins
  • Reflectivity
  • Self-assembly


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