User:Finn Aachmann

I defined my MSc project based on the knowledge gap for the interaction between cyclodextrin and proteins and setup my supervisor team Kim L. Larsen, Daniel E. Ozten and Reinhard Wimmer. Here I chose NMR spectroscopy as the main method to study the inclusion complex formation between cyclodextrin and proteins due to its ability to give atomic level information. I obtained MSc in Biotechnology at Aalborg University (Denmark) in 2001 [1, 2, 3].

The main focus of my PhD project was acquiring a deeper insight into structure elucidation with NMR and I started to work on alginate C-5 epimerases 2002-2005 in a collaboration between Svein Valla at NTNU (Norwegian University of Science and Technology) and Reinhard Wimmer at Aalborg University [4, 5, 6]. Besides using NMR, I also focus on functional characterization of the alginate epimerases (using ITC, CD, FS and protein engineering) to understand ionic and substrate/product interaction, mode of action and role of the subunits in the alginate epimerases.

During my Post Doc at NTNU (2005-2007) I continued with structure elucidation and functional characterization on selenocysteine containing proteins using NMR spectroscopy under the supervision of Alex Dykyy at NTNU. Here I also had a key role in building up the NMR structure determination facilities at the NV-faculty NMR center NTNU and today I lead the NMR laboratory.

I was recruited as senior scientist on structure elucidation of proteins and carbohydrates by NMR in NOBIPOL (The Norwegian Biopolymer Laboratory) at NTNU (2007-2016). During this period, we started a collaboration with Vincent Eijsink with focus on structure and functional determination of lytic polysaccharide monooxygenases (LPMO) with NMR [7, 8, 9, 10, 11, 12]. Here we used NMR in many ways, not only to obtain the structure, but also to get functional insight into the LPMOs and their products. Besides the LPMO we also continued to work with alginate epimerases and became interested in the chemo-enzymatic functionalization of alginate and other carbohydrates as well as the characterization thereof [13, 14, 15, 16, 17, 18, 19, 20]. The versatility of NMR is also shown in our work following enzymatic or chemical transformation in the NMR tube [21, 22].

Today, I’m leading Biopolymer NMR group at NTNU and we focus on structure and functional characterization on polysaccharides, carbohydrate modifying enzymes, multidomain proteins and biomaterials.

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References

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7. Aachmann FL, Sørlie M, Skjåk-Bræk G, Eijsink VG, and Vaaje-Kolstad G. (2012). NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions. Proc Natl Acad Sci U S A. 2012;109(46):18779-84. DOI:10.1073/pnas.1208822109 |
9. Isaksen T, Westereng B, Aachmann FL, Agger JW, Kracher D, Kittl R, Ludwig R, Haltrich D, Eijsink VG, and Horn SJ. (2014). A C4-oxidizing lytic polysaccharide monooxygenase cleaving both cellulose and cello-oligosaccharides. J Biol Chem. 2014;289(5):2632-42. DOI:10.1074/jbc.M113.530196 |
10. Courtade G, Wimmer R, Røhr ÅK, Preims M, Felice AK, Dimarogona M, Vaaje-Kolstad G, Sørlie M, Sandgren M, Ludwig R, Eijsink VG, and Aachmann FL. (2016). Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase. Proc Natl Acad Sci U S A. 2016;113(21):5922-7. DOI:10.1073/pnas.1602566113 |