Abstract
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 language | English |
|---|---|
| Pages (from-to) | s355-s360 |
| Journal | Journal of Applied Crystallography |
| Volume | 40 |
| Issue number | Part s1 |
| DOIs | |
| Publication status | Published - 2007 |
| MoE publication type | A1 Journal article-refereed |
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Keywords
- hydrophobins
- grazing-incidence X-ray diffraction
- self-assembly
- reflectivity
Cite this
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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 journal › Article › Scientific › peer-review
TY - JOUR
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
PY - 2007
Y1 - 2007
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.
KW - hydrophobins
KW - grazing-incidence X-ray diffraction
KW - self-assembly
KW - reflectivity
U2 - 10.1107/S0021889807001331
DO - 10.1107/S0021889807001331
M3 - Article
VL - 40
SP - s355-s360
JO - Journal of Applied Crystallography
JF - Journal of Applied Crystallography
SN - 0021-8898
IS - Part s1
ER -