Self-assembled films of hydrophobin protein HFBIII from Trichoderma reesei

Kaisa Kisko (Corresponding Author), Géza Szilvay, Elina Vuorimaa, Helge Lemmetyinen, Markus Linder, Mika Torkkeli, Ritva Serimaa

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, [gamma] = 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)s355-s360
JournalJournal of Applied Crystallography
Issue numberPart s1
Publication statusPublished - 2007
MoE publication typeA1 Journal article-refereed


  • hydrophobins
  • grazing-incidence X-ray diffraction
  • self-assembly
  • reflectivity

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