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里氏木霉疏水蛋白HFBI的溶液缔合与表面活性之间的关系。

The relation between solution association and surface activity of the hydrophobin HFBI from Trichoderma reesei.

作者信息

Szilvay Géza R, Kisko Kaisa, Serimaa Ritva, Linder Markus B

机构信息

VTT, Technical Research Centre of Finland, Finland.

出版信息

FEBS Lett. 2007 Jun 12;581(14):2721-6. doi: 10.1016/j.febslet.2007.05.024. Epub 2007 May 21.

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.

摘要

疏水蛋白是一类小型真菌表面活性蛋白,它们在界面处自组装成具有纳米级结构的薄膜。里氏木霉的疏水蛋白HFBI已被证明在溶液中会缔合成四聚体,但这种缔合对HFBI功能的作用仍不清楚。我们制备了两种HFBI变体,它们在溶液中的缔合平衡显著向四聚体状态偏移。然而,这种增强的溶液缔合并没有改变变体HFBI的表面性质。结果表明,HFBI的溶液缔合状态与诸如表面活性等表面性质之间没有很强的关系。

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