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.
Original language | English |
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Pages (from-to) | 355-360 |
Number of pages | 6 |
Journal | Journal of Applied Crystallography |
Volume | 40 |
DOIs | |
Publication status | Published - Apr 2007 |
MoE publication type | A1 Journal article-refereed |
Keywords
- Grazing-incidence X-ray diffraction
- Hydrophobins
- Reflectivity
- Self-assembly