Hydrophobin film structure for HFBI and HFBII and mechanism for accelerated film formation.

Autor: Aniket Magarkar, Nawel Mele, Noha Abdel-Rahman, Sarah Butcher, Mika Torkkeli, Ritva Serimaa, Arja Paananen, Markus Linder, Alex Bunker

Publikováno v: PLoS Computational Biology, Vol 10, Iss 7, p e1003745 (2014)

Hydrophobins represent an important group of proteins from both a biological and nanotechnological standpoint. They are the means through which filamentous fungi affect their environment to promote growth, and their properties at interfaces have resu

Externí odkaz: https://doaj.org/article/b56968f9c7bb4ed59e9f317b05fc2240

Lignin nanoparticles modified with tall oil fatty acid for cellulose functionalization

Autor: Monika Österberg, Géza R. Szilvay, Arja Paananen, Ville Liljeström, Eva-Lena Hult, Hanna-Leena Alakomi, Kalle Lintinen, Miriam Kellock, Miikka Lievonen, Mauri A. Kostiainen, Harri Setälä

Publikováno v: Setälä, H, Alakomi, H-L, Paananen, A, Szilvay, G, Kellock, M, Lievonen, M, Liljeström, V, Hult, E-L, Lintinen, K, Österberg, M & Kostiainen, M A 2020, ' Lignin nanoparticles modified with tall oil fatty acid for cellulose functionalization ', Cellulose, vol. 27, pp. 273-284 . https://doi.org/10.1007/s10570-019-02771-9

In this study, tall oil fatty acid ester of softwood kraft lignin (TOFA-L) was used to prepare TOFA lignin nanoparticles (TLNP) in water. The average diameters for two prepared TLNPs in 0.1 mg/ml concentration were 140 nm and 160 nm. TLNPs were attac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc6ce95c8f8f1b5ba3b2e67951408459
https://doi.org/10.1007/s10570-019-02771-9

Lab Cultured Meats

Autor: Dilek Ercili-Cura, Toni Ryynänen, Arja Paananen, Dorothee Barth

Publikováno v: ACS In Focus ISBN: 9780841299085
ACS In Focus

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b744cc94621223360765be9975a4fecd
https://doi.org/10.1021/acs.infocus.7e4007

Single-Molecule Force Spectroscopy Reveals Self-Assembly Enhanced Surface Binding of Hydrophobins

Autor: Arja Paananen, Yi Cao, Géza R. Szilvay, Xin Wang, Wei Wang, Bing Li, Ying Li, Meng Qin

Publikováno v: Li, B, Wang, X, Li, Y, Paananen, A, Szilvay, G R, Qin, M, Wang, W & Cao, Y 2018, ' Single-Molecule Force Spectroscopy Reveals Self-Assembly Enhanced Surface Binding of Hydrophobins ', Chemistry-A European Journal, vol. 24, no. 37, pp. 9224-9228 . https://doi.org/10.1002/chem.201801730

Hydrophobins have raised lots of interest as powerful surface adhesives. However, it remains largely unexplored how their strong and versatile surface adhesion is linked to their unique amphiphilic structural features. Here, we develop an AFM-based s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96aa212a69384fbf320a24335bd12cc6
https://doi.org/10.1002/chem.201801730

Molecular structure of hydrophobins studied with site-directed mutagenesis and vibrational sum-frequency generation spectroscopy

Autor: Huib J. Bakker, Bart Speet, Arja Paananen, Konrad Meister, Michael Lienemann

Publikováno v: Meister, K, Paananen, A, Speet, B, Lienemann, M & Bakker, H 2017, ' Molecular structure of hydrophobins studied with site-directed mutagenesis and vibrational sum-frequency generation spectroscopy ', The Journal of Physical Chemistry B, vol. 121, no. 40, pp. 9398-9402 . https://doi.org/10.1021/acs.jpcb.7b08865
The Journal of Physical Chemistry. B

Hydrophobins are surface-active fungal proteins that adsorb to the water-air interface and self-assemble into amphiphilic, water-repelling films that have a surface elasticity that is an order of magnitude higher than other molecular films. Here we u

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d43171716326e12480c606a8d293d287
https://doi.org/10.1021/acs.jpcb.7b08865