ArticleBiophysical journal2008
Interactions of hydrophobin proteins in solution studied by small-angle X-ray scattering.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 56 citations in OpenAlex.
- AlphaFold modeling uncovers global structural features of class I and class II fungal hydrophobins.Protein science : a publication of the Protein Society · 2025Article
- A novel strategy for production of liraglutide precursor peptide and development of a new long-acting incretin mimic.PloS one · 2022Article
- Vibrio cholerae biofilm scaffolding protein RbmA shows an intrinsic, phosphate-dependent autoproteolysis activity.IUBMB life · 2021Article
- Observation of pH-Induced Protein Reorientation at the Water Surface.The journal of physical chemistry letters · 2017Article
- Induced Fit in Protein Multimerization: The HFBI Case.PLoS computational biology · 2016Article
- Recent Advances in Fungal Hydrophobin Towards Using in Industry.The protein journal · 2015Review
- Diffusion of hydrophobin proteins in solution and interactions with a graphite surface.BMC biophysics · 2011Article
- Bioactive modification of silicon surface using self-assembled hydrophobins from Pleurotus ostreatus.The European physical journal. E, Soft matter · 2009Article
- Quantifying biomolecular hydrophobicity: Single molecule force spectroscopy of class II hydrophobins.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrophobins are a group of very surface-active, fungal proteins known to self-assemble on various hydrophobic/hydrophilic interfaces. The self-assembled films coat fungal structures and mediate their attachment to surfaces. Hydrophobins are also soluble in water. Here, the association of hydrophobins HFBI and HFBII from Trichoderma reesei in aqueous solution was studied using small-angle x-ray scattering. Both HFBI and HFBII exist mainly as tetramers in solution in the concentration range 0.5-10 mg/ml. The assemblies of HFBII dissociate more easily than those of HFBI, which can tolerate changes of pH from 3 to 9 and temperatures in the range 5 degrees C-60 degrees C. The self-association of HFBI and HFBII is mainly driven by the hydrophobic effect, and addition of salts along the Hofmeister series promotes the formation of larger assemblies, whereas ethanol breaks the tetramers into monomers. The possibility that the oligomers in solution form the building blocks of the self-assembled film at the air/water interface is discussed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.