Prof. Dr. Arnold Boersma
The Boersma group focusses on synthetic biochemistry, to engineer new proteins as well as larger cell-like systems. These systems are synthesized with specific applications in mind, which range from medical relevance (diagnosis, screening and/or understanding the basis of disease) to materials and devices. The group has especially a strong record of accomplishment on the design of FRET-based protein probes for macromolecular crowding in diverse living and nonliving systems and for ionic strength measurements. Current interests lie in the development of novel probes and cell-like systems to detect novel parameters in fields that range from biology to material science.
Curriculum Vitae
Dr. Arnold J. Boersma studied chemistry at the University of Groningen (The Netherlands) where he also pursued his graduate studies in the group of Prof. Ben L. Feringa (Nobel Laureate, 2016) and Prof. Gerard Roelfes. Here, he developed a new concept in catalysis by using DNA as an asymmetric catalyst. For this research, he was awarded the KNCV Catalysis prize for the best PhD thesis on catalysis in the Netherlands. He then worked as a postdoctoral fellow at Oxford University in the group of Prof. Hagan Bayley, funded by an NWO Rubicon grant. Here, he became an expert in protein engineering and lipid membranes. In 2012, he returned to the University of Groningen to become an independent researcher with an NWO Veni fellowship. Here, he developed novel probes to detect the physicochemical properties in various types of cells. Based on these research achievements he was awarded an NWO Vidi fellowship in 2016 to become a group leader. He joined the DWI-Leibniz Institute for Interactive Materials in August 2018.
Selected professional functions, honors and awards
- 2021 Fellow Max Planck School "Matter to Life"
- 2020 ACS Sensors selected "Rising stars in sensing"
- 2020 Consolidator Grant of the ERC
- 2016 Vidi grant der Netherlands Organization for Scientific Research (NWO)
- 2012 Veni grant of the NOW
- 2011 KNCV Catalysis prize for the best doctoral thesis in the field of catalysis in the Netherlands in 2009-2010
- 2009 Presentation of the "Cum Laude" award (top 5%) for the doctoral thesis
- 2009 Rubicon grant of the NOW
Projects
Publications
| Titel/Autoren | DOI-LINK | Magazine | Jahre | |
|---|---|---|---|---|
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Cell Wall Damage Increases Macromolecular Crowding Effects in the Escherichia Coli Cytoplasm
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https://doi.org/10.1016/j.isci.2023.106367 | iScience | 2023 | |
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A Fret-Based Method for Monitoring Structural Transitions in Protein Self-Organization
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https://doi.org/10.1016/j.crmeth.2022.100184 | Cell Reports Methods | 2022 | |
|
High Macromolecular Crowding in Liposomes from Microfluidics
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https://doi.org/10.1002/advs.202201169 | Advanced Science | 2022 | |
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A Precise and General Fret-Based Method for Monitoring Structural Transitions in Protein Self-Organization
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https://doi.org/10.1101/2021.02.25.432866 | bioRxiv | 2021 | |
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Activation of the Catalytic Activity of Thrombin for Fibrin Formation by Ultrasound
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https://doi.org/10.1002/anie.202105404 | Angewandte Chemie International Edition | 2021 | |
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Characterization of a New hetero-FRET Biosensor to Measure Environmental Ionic Strength
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https://doi.org/10.1016/j.bpj.2020.11.967 | Biophysical Journal | 2021 | |
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Effect of Donor Identity on FRET Sensor Sensitivity to Environmental Macromolecular Crowding
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https://doi.org/10.1016/j.bpj.2020.11.966 | Biophysical Journal | 2021 | |
|
Fluorescence depolarization dynamics of ionic strength sensors using time-resolved anisotropy
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https://doi.org/10.1016/j.bpj.2021.01.035 | Biophysical Journal | 2021 | |
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Molecular Brightness Approach for Fret Analysis of Donor-Linker-Acceptor Constructs at the Single Molecule Level: A Concept
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https://doi.org/10.3389/fmolb.2021.730394 | Frontiers in Molecular Biosciences | 2021 | |
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A physicochemical perspective of aging from single-cell analysis of pH, macromolecular and organellar crowding in yeast
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https://doi.org/10.7554/eLife.54707 | eLife | 2020 | |
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Chapter Three - Engineering crowding sensitivity into protein linkers
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https://doi.org/10.1016/bs.mie.2020.09.007 | Methods in Enzymology [Book] | 2020 | |
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Comparative Photophysical Studies of mCerulean3 and mTurquoise2.1 as FRET Donors
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https://doi.org/10.1016/j.bpj.2019.11.423 | Biophysical Journal | 2020 |
