Abstract
Hydrophobins are small fungal surface active proteins that self-assemble
at interfaces into films with nanoscale structures. The hydrophobin HFBI from
Trichoderma reesei has been shown to associate in solution into tetramers but
the role of this association on the function of HFBI has remained unclear. We
produced two HFBI variants that showed a significant shift in solution
association equilibrium towards the tetramer state. However, this enhanced
solution association did not alter the surface properties of the variant
HFBIs. The results show that there is not a strong relationship between HFBI
solution association state and surface properties such as surface activity.
Original language | English |
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Pages (from-to) | 2721-2726 |
Journal | FEBS Letters |
Volume | 581 |
Issue number | 14 |
DOIs | |
Publication status | Published - 2007 |
MoE publication type | A1 Journal article-refereed |
Keywords
- hydrophobins
- Protein multimerization
- Protein self-assembly
- Surface active protein