Self-assembled films of hydrophobin protein HFBIII from Trichoderma reesei

Research output: Contribution to journalArticleScientificpeer-review

Researchers

  • Kaisa Kisko
  • Géza R. Szilvay
  • Elina Vuorimaa
  • Helge Lemmetyinen
  • Markus Linder

  • Mika Torkkeli
  • Ritva Serimaa

Research units

  • VTT Technical Research Centre of Finland
  • University of Helsinki
  • Tampere University of Technology

Abstract

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.

Details

Original languageEnglish
Pages (from-to)355-360
Number of pages6
JournalJournal of Applied Crystallography
Volume40
Publication statusPublished - Apr 2007
MoE publication typeA1 Journal article-refereed

    Research areas

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

ID: 4806079