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.
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 |
Keywords
- hydrophobins
- grazing-incidence X-ray diffraction
- self-assembly
- reflectivity