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

15 Citations (Scopus)

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, [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
Volume40
Issue numberPart s1
DOIs
Publication statusPublished - 2007
MoE publication typeA1 Journal article-refereed

Fingerprint

Trichoderma
Cysteine
Proteins
Coatings
Silicon
Fungi
X-Ray Diffraction
Disulfides
Self assembly
Lattice constants
Monolayers
Catalytic Domain
Air
Crystalline materials
X ray diffraction
Water
Incidence
Substrates

Keywords

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

Cite this

Kisko, K., Szilvay, G., Vuorimaa, E., Lemmetyinen, H., Linder, M., Torkkeli, M., & Serimaa, R. (2007). Self-assembled films of hydrophobin protein HFBIII from Trichoderma reesei. Journal of Applied Crystallography, 40(Part s1), s355-s360. https://doi.org/10.1107/S0021889807001331
Kisko, Kaisa ; Szilvay, Géza ; Vuorimaa, Elina ; Lemmetyinen, Helge ; Linder, Markus ; Torkkeli, Mika ; Serimaa, Ritva. / Self-assembled films of hydrophobin protein HFBIII from Trichoderma reesei. In: Journal of Applied Crystallography. 2007 ; Vol. 40, No. Part s1. pp. s355-s360.
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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 {\AA}, [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.",
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Kisko, K, Szilvay, G, Vuorimaa, E, Lemmetyinen, H, Linder, M, Torkkeli, M & Serimaa, R 2007, 'Self-assembled films of hydrophobin protein HFBIII from Trichoderma reesei', Journal of Applied Crystallography, vol. 40, no. Part s1, pp. s355-s360. https://doi.org/10.1107/S0021889807001331

Self-assembled films of hydrophobin protein HFBIII from Trichoderma reesei. / Kisko, Kaisa (Corresponding Author); Szilvay, Géza; Vuorimaa, Elina; Lemmetyinen, Helge; Linder, Markus; Torkkeli, Mika; Serimaa, Ritva.

In: Journal of Applied Crystallography, Vol. 40, No. Part s1, 2007, p. s355-s360.

Research output: Contribution to journalArticleScientificpeer-review

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T1 - Self-assembled films of hydrophobin protein HFBIII from Trichoderma reesei

AU - Kisko, Kaisa

AU - Szilvay, Géza

AU - Vuorimaa, Elina

AU - Lemmetyinen, Helge

AU - Linder, Markus

AU - Torkkeli, Mika

AU - Serimaa, Ritva

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N2 - 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.

AB - 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.

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