Markus B Linder
Affiliation: VTT Biotechnology
- Design of a pH-dependent cellulose-binding domainM Linder
VTT Biotechnology and Food Research, Finland
FEBS Lett 447:13-6. 1999..Although the binding of the mutants at optimal pH was less than for the wild-type, in one case, Y31H, this binding almost reached the wild-type level...
- The hydrophobins HFBI and HFBII from Trichoderma reesei showing efficient interactions with nonionic surfactants in aqueous two-phase systemsM Linder
VTT Biotechnology, P O Box 1500, FIN 02044 VTT, Finland and Institute für Enzymtechnologie der Heinrich Heine Universität Düsseldorf, Forschungszentrum Julich, D 52426 Jülich, Germany
Biomacromolecules 2:511-7. 2001..The use of this method for purifying the proteins from crude fungal culture supernatants is demonstrated and implications of the protein-polymer interaction are discussed...
- Hydrophobins: the protein-amphiphiles of filamentous fungiMarkus B Linder
VTT Biotechnology, Tietotie 2, P O Box 1500, FIN 02044 VTT, Finland
FEMS Microbiol Rev 29:877-96. 2005..In this review, the properties of hydrophobins are analyzed in light of these new data. Various application possibilities are also discussed...
- Efficient purification of recombinant proteins using hydrophobins as tags in surfactant-based two-phase systemsMarkus B Linder
VTT Biotechnology, Technical Research Centre of Finland, P O Box 1500, FIN 02044 VTT, Finland
Biochemistry 43:11873-82. 2004..This unusually strong and specific interaction between polymeric surfactants and a soluble protein shows promise for new developments in interfacing proteins and nonbiological materials for other applications as well...
- Selective nanopatterning using citrate-stabilized Au nanoparticles and cystein-modified amphiphilic proteinPäivi Laaksonen
VTT Biotechnology, VTT Technical Research Centre of Finland, FI 02044 VTT Espoo, Finland
Langmuir 25:5185-92. 2009....
- The relation between solution association and surface activity of the hydrophobin HFBI from Trichoderma reeseiGeza R Szilvay
VTT, Technical Research Centre of Finland, Finland
FEBS Lett 581:2721-6. 2007..The results show that there is not a strong relationship between HFBI solution association state and surface properties such as surface activity...
- Mechanisms of protein adhesion on surface films of hydrophobinZefang Wang
VTT Biotechnology, Technical Research Centre of Finland, Tietotie 2, FIN 02044VTT, Espoo, Finland
Langmuir 26:8491-6. 2010..We conclude that hydrophobins can transform a nonpolar surface into one that efficiently recruits other proteins by charge interactions...
- Behavior of Trichoderma reesei hydrophobins in solution: interactions, dynamics, and multimer formationGeza R Szilvay
VTT Biotechnology, Tietotie 2, P O Box 1000, FIN 02044 VTT, Finland
Biochemistry 45:8590-8. 2006..In contrast to micelles formed by detergents, the hydrophobin multimers are defined in size and involve specific protein-protein interactions...
- Self-assembled hydrophobin protein films at the air-water interface: structural analysis and molecular engineeringGeza R Szilvay
VTT Technical Research Centre of Finland, P O Box 1000, FI 02044 VTT, Espoo, Finland
Biochemistry 46:2345-54. 2007..The interactions between the proteins in the network are likely to be responsible for the unusual surface elasticity of the hydrophobin film...
- Genetic engineering in biomimetic compositesPäivi Laaksonen
VTT Nanobiomaterials, VTT Technical Research Centre of Finland, Tietotie 2, Espoo, P O Box 1000, FI 02044, Finland
Trends Biotechnol 30:191-7. 2012..This field is emerging but has already shown promising results and much progress in the next few years is expected...
- Self-assembly of class II hydrophobins on polar surfacesMathias S Grunér
VTT Technical Research Centre of Finland, Biotechnology, Espoo, Finland
Langmuir 28:4293-300. 2012..The results are significant for understanding the mechanism for formation of structures such as the surface of mycelia or fungal spore coatings as well as for possible technical applications...
- Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamianaJussi J Joensuu
VTT Biotechnology, VTT Technical Research Centre of Finland, Espoo, 02044 VTT, Finland
Plant Physiol 152:622-33. 2010..This hydrophobin fusion technology, when combined with the speed and posttranslational modification capabilities of plants, enhances the value of transient plant-based expression systems...
- Enhanced plastic deformations of nanofibrillated cellulose film by adsorbed moisture and protein-mediated interactionsJani Markus Malho
VTT Technical Research Centre of Finland, Tietotie 2, P O Box 1000, FI 02044, Espoo, Finland
Biomacromolecules 16:311-8. 2015..The work helps to understand the functional basis of nanocellulose composites as materials and aims toward building model systems for molecular biomimetic materials. ..
- Charge-Based Engineering of Hydrophobin HFBI: Effect on Interfacial Assembly and InteractionsMichael Lienemann
VTT Technical Research Centre of Finland, Tietotie 2, FI 02150 Espoo, Finland
Biomacromolecules 16:1283-92. 2015....
- Immobilization-stabilization of proteins on nanofibrillated cellulose derivatives and their bioactive film formationSuvi Arola
VTT, Technical Research Centre of Finland, Bio and Process Technology, Tietotie 2, P O Box 1000, FIN 02044 VTT, Finland
Biomacromolecules 13:594-603. 2012..This allows more scalable methods and better control of conditions compared to the traditional methods that depend on surface reactions...
- Controlled hybrid nanostructures through protein-mediated noncovalent functionalization of carbon nanotubesKatri Kurppa
VTT Biotechnology, VTT Technical Research Centre of Finland, Tietotie 2, P O Box 1000, 02044 Espoo, Finland
Angew Chem Int Ed Engl 46:6446-9. 2007
- Structural hierarchy in molecular films of two class II hydrophobinsArja Paananen
VTT Biotechnology, Technical Research Centre of Finland, P O Box 1500, FIN 02044 VTT, Espoo, Finland
Biochemistry 42:5253-8. 2003..The possibility that the highly organized surface assemblies of hydrophobins could allow a route for manufacturing functional surfaces is suggested...
- Atomic resolution structure of the HFBII hydrophobin, a self-assembling amphiphileJohanna Hakanpaa
Department of Chemistry, University of Joensuu, PO Box 111, 80101 Joensuu, Finland
J Biol Chem 279:534-9. 2004..The data presented show that much of the current views on structure function relations in hydrophobins must be re-evaluated...
- Interactions of hydrophobin proteins in solution studied by small-angle X-ray scatteringKaisa Kisko
Department of Physical Sciences, University of Helsinki, FI 00014 HU, Finland
Biophys J 94:198-206. 2008..The possibility that the oligomers in solution form the building blocks of the self-assembled film at the air/water interface is discussed...
- Crystal structures of hydrophobin HFBII in the presence of detergent implicate the formation of fibrils and monolayer filmsJohanna M Kallio
Department of Chemistry, University of Joensuu, P O Box 111, 80101 Joensuu, Finland
J Biol Chem 282:28733-9. 2007..We propose that the structure of the fibrils and/or rodlets is similar to that observed in the crystal structure...
- Protein HGFI from the edible mushroom Grifola frondosa is a novel 8 kDa class I hydrophobin that forms rodlets in compressed monolayersLei Yu
College of Life Sciences, Nankai University, No 94 Weijin Road, Tianjin 300071, PR China
Microbiology 154:1677-85. 2008..Most rodlets were aligned in the same direction, indicating that formation of rodlets may be promoted during compression of the monolayer...
- Hydrophobin (HFBI): A potential fusion partner for one-step purification of recombinant proteins from insect cellsTomi Lahtinen
Department of Biological and Environmental Science, University of Jyvaskyla, Nanoscience Center, PO Box 35, 40014 Jyvaskyla, Finland
Protein Expr Purif 59:18-24. 2008....
- Multivalent dendrons for high-affinity adhesion of proteins to DNAMauri A Kostiainen
Department of Engineering Physics and Mathematics and Center for New Materials, Helsinki University of Technology, P O BOX 2200, 02015 HUT, Espoo, Finland
Angew Chem Int Ed Engl 45:3538-42. 2006
- Cleavage of recombinant proteins at poly-His sequences by Co(II) and Cu(II)Martina Andberg
VTT Technical Research Centre of Finland, Espoo FIN 02044 VTT, Finland
Protein Sci 16:1751-61. 2007..The work described here can also have implications for understanding protein stability in vitro and in vivo...