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Self‐assembled films of hydrophobin protein HFBIII from Trichoderma reesei
Author(s) -
Kisko Kaisa,
Szilvay Géza R.,
Vuorimaa Elina,
Lemmetyinen Helge,
Linder Markus B.,
Torkkeli Mika,
Serimaa Ritva
Publication year - 2007
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889807001331
Subject(s) - hydrophobin , trichoderma reesei , monolayer , chemistry , residue (chemistry) , crystallography , amphiphile , cysteine , fungal protein , materials science , organic chemistry , biochemistry , polymer , enzyme , cellulase , yeast , saccharomyces cerevisiae , gene , copolymer
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.