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Large equipment

High-Speed Aromic Force Microscope

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University of Applied Sciences Upper Austria

Linz | Website

Open for Collaboration

Short Description

High-speed atomic force microscopy enables the label-free visualization of individual biological molecules (proteins, membranes, DNA, RNA, etc.), their interactions and dynamics, as well as conformational changes in their natural context, i. in aqueous environment and at physiological temperatures, with sub-molecular spatial and 100 ms time resolution.

Contact Person

Johannes Preiner

Research Services

»Analysis of molecular interactions and physical surface properties
Chemical rates constants and affinities, stoichiometry, multivalency, interaction forces and energies
»Label-free real-time visualization of biomolecules, interactions and conformational changes, cellular interaction studies (drug characterization)
»Combination of results and modeling, mathematical modeling and simulation

Methods & Expertise for Research Infrastructure

Various applications in the field of dynamics and interactions of soluble proteins and membrane proteins, antibody-antigen interactions, complement activation, exosomes, viruses, etc.

Terms of Use

For details please contact the project leader.

Reference Publications

1. M. Axmann, E. Sezgin, A. Karner, J. Novacek, M.D. Brodesser, C. Röhrl, J. Preiner, H. Stangl, B. Plochberger. „Receptor-independent transfer of low density lipoprotein cargo to bio-membranes“ Nano Letters (2019)

2. B. Plochberger, C. Röhrl, J. Preiner, C. Rankl, M. Brameshuber, J. Madl, R. Bittman, R. Ros, E. Sezgin, C. Eggeling, P. Hinterdorfer, H. Stangl, G. J. Schütz „HDL particles incorporate into lipid bilayers – a combined AFM and single molecule fluorescence microscopy study” Scientific Reports 7 (15886) (2017)
doi:10.1038/s41598-017-15949-7

3. A. Karner, B. Nimmervoll, B. Plochberger, E. Klotzsch, A. Horner, D.G. Knyazev, R. Kuttner, K. Winkler, L. Winter, C. Siligan, N. Ollinger, P. Pohl, J. Preiner* „Tuning membrane protein mobility by confinement into nanodomains“ Nature Nanotechnology 12(3) (2017)
doi:10.1038/nnano.2016.236

4. B. Nimmervoll, L. A. Chtcheglova, K. Juhasz, N. Cremades, F. A. Aprile, A. Sonnleitner, P. Hinterdorfer, L. Vigh, J. Preiner, Z. Balogi „Cell surface localised Hsp70 is a cancer specific regulator of clathrin-independent endocytosis“ FEBS Letters, 589 (19B) (2015)
doi: 10.1016/j.febslet.2015.07.037

5. A. Horner‡ F. Zocher‡ J. Preiner‡ N. Ollinger, C. Siligan, Sergey A. Akimov, P. Pohl „The mobility of single‐file water molecules is governed by the number of H‐bonds they may form with channel‐ lining residues“ Science Advances 2 (2015) doi: 10.1126/sciadv.1400083

6. J. Preiner*, A. Horner, A. Karner, N. Ollinger, C. Siligan, P. Pohl, P. Hinterdorfer „High-Speed AFM Images of Thermal Motion Provide Stiffness Map of Interfacial Membrane Protein Moieties “Nano Letters 15 (2014) doi: 10.1021/nl504478f

7. J. Preiner, N. Kodera, J. Tang, A. Ebner, M. Brameshuber, D. Blaas, N. Gelbmann, H.J. Gruber, T. Ando, P. Hinterdorfer „IgGs are made for walking on bacterial and viral surfaces“ Nature Communications 5 (2014) doi: 10.1038/ncomms5394

Contact

Dr
Johannes Preiner
0043 5 0804 55073
johannes.preiner@fh-linz.at
https://research.fh-ooe.at/de/staff/48286?tab=2

Location

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