The dynamics of multimer formation of the amphiphilic hydrophobin protein HFBII.

摘要: Hydrophobins are surface-active proteins produced by filamentous fungi. They have amphiphilic structures and form multimers in aqueous solution to shield their hydrophobic regions. The rearrange at interfaces self-assemble into films that can show a very high degree of structural order. Little is known on dynamics multimer interactions how this affected other components. In work we examine the stopped-flow fluorescence measurements Forster Resonance Energy Transfer (FRET) using class II hydrophobin HFBII. half-life exchange state was 0.9s 22°C with an activation energy 92kJ/mol. process HFBII shown be significantly closely related HFBI hydrophobin, lowering both for exchange. Lower molecular weight surfactants interacted selective ways, but surface active did not influence rates results indicate formation driven specific distinguish different hydrophobins from each other.