• E-mailArne.Raasakka@uib.no
  • Visitor Address
    Jonas Lies vei 91
  • Postal Address
    Postboks 7804
    5020 Bergen

I'm a postdoctoral research fellow in the Neurotargeting Research Group at the Department of Biomedicine, Faculty of Medicine, working under the research project of Professor Petri Kursula.

My scientific background and research interests are in structural neurobiochemistry, with particular emphasis on the molecular foundation of myelin stability, myelin formation, and demyelination. More specifically, the research project aims to uncover the structure-function relationships of highly abundant myelin proteins, such as myelin basic protein, myelin protein zero, and periaxin. These proteins, all of which have relevance in the etiology of incurable demyelinating diseases, ensure the correct function of myelin as a nerve insulator in our central and peripheral nervous systems.

My practical research expertise is in protein science, especially involving enzymes, intrinsically disordered proteins, and membrane-binding proteins. My methodological skills are centered on the biophysical in vitro charaterization of protein-membrane model systems using protein X-ray crystallography, small-angle X-ray scattering, circular dichroism methods, as well as others. An exhaustive list can be found under the Background tab.

h-index: 9 (Web of Science)

Publications: 26 (last 5 years: 19)



  • Mahootchi E.*, Raasakka A.*, Luan W., Muruganandam G., Loris R., Haavik J. & Kursula P. (2021) Structure and substrate specificity determinants of the taurine biosynthetic enzyme cysteine sulphinic acid decarboxylase. J Struct Biol. 213(1): 107674. doi: 10.1016/j.jsb.2020.107674.

  • Nguyen G.T.T.*, Sutinen A.*, Raasakka A., Muruganandam G., Loris R. & Kursula P. (2021) Structure of the complete dimeric human GDAP1 core domain provides insights into ligand binding and clustering of disease mutations. Front Mol Biosci. 7: 631232. doi: 10.3389/fmolb.2020.631232.

  • Myllykoski M., Sutinen A., Koski K., Kallio J.P., Raasakka A., Myllyharju J.,  Wierenga R.K. & Koivunen P. (2021) Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains. J Biol Chem. 296: 100197. doi: 10.1074/jbc.RA120.016542.


  • Raasakka A. & Kursula P. (2020) How Does Protein Zero Assemble Compact Myelin? Cells 9(8): 1832. doi: 10.3390/cells9081832. Part of the special issue "Schwann Cells: From Formation to Clinical Significance". Review.

  • Ruskamo S.*, Krokengen O.C.*, Kowal J., Nieminen T., Lehtimäki M., Raasakka A., Dandey V., Vattulainen I., Stahlberg H. & Kursula P. (2020) Cryo-EM, X-ray diffraction, and atomistic simulations reveal determinants for the formation of a supramolecular myelin-like proteolipid lattice. J Biol Chem. 295: 8692-8705. doi: 10.1074/jbc.RA120.013087.

  • Lillebostad P.A.G.*, Raasakka A.*, Hjellbrekke S.J., Patil S., Røstbø T., Hollås H., Sakya S.A., Szigetvari P.D., Vedeler A. & Kursula P. (2020) Structure of the ALS Mutation Target Annexin A11 Reveals a Stabilising N-Terminal Segment. Biomolecules 10(4): 660. doi: 10.3390/biom10040660. Part of the special issue "Metal Binding Proteins 2020".

  • Raasakka A. & Kursula P. (2020) Flexible Players within the Sheaths: The Intrinsically Disordered Proteins of Myelin in Health and Disease. Cells 9(2): 470. doi: 10.3390/cells9020470. Part of the special issue "Structure and Function of Healthy and Diseased Myelin". Review.


  • Raasakka A. & Kursula P. (2019) Stability and flexibility of full-length human oligodendrocytic QKI6. BMC Res Notes. 12: 609. doi: 10.1186/s13104-019-4629-x.

  • Raasakka A., Ruskamo S., Barker R., Krokengen O.C., Vatne G.H., Kristiansen C.K., Hallin E.I., Skoda M.W.A., Bergmann U., Wacklin-Knecht, H., Jones N.C., Hoffmann S.V & Kursula P. (2019) Neuropathy-related mutations alter the membrane binding properties of the human myelin protein P0 cytoplasmic tail. PLoS ONE 14(6): e0216833. doi: 10.1371/journal.pone.0216833.

  • Raasakka A., Linxweiler H., Brophy P.J., Sherman D.L. & Kursula P. (2019) Direct binding of the flexible C-terminal segment of periaxin to β4 integrin suggests a molecular basis for CMT4F. Front Mol Neurosci. 12: 84. doi: 10.3389/fnmol.2019.00084.

  • Raasakka A., Jones N.C., Hoffmann S.V. & Kursula P. (2019) Ionic strength and calcium regulate the membrane interactions of myelin basic protein and the cytoplasmic domain of myelin protein zero. Biochem Biophys Res Commun. 511(1): 7-12. doi: 10.1016/j.bbrc.2019.02.025.

  • Raasakka A., Ruskamo S., Kowal J., Han H., Baumann A., Myllykoski M., Fasano A., Rossano R., Riccio P., Bürck J., Ulrich A.S., Stahlberg H. & Kursula P. (2019) Molecular structure and function of myelin protein P0 in membrane stacking. Sci Rep. 9: 642. doi: 10.1038/s41598-018-37009-4.


  • Laulumaa S., Nieminen T., Raasakka A., Krokengen O.C., Safaryan A., Hallin E.I., Brysbaert G., Lensink M.F., Ruskamo S., Vattulainen I. & Kursula P. (2018) Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins. BMC Struct Biol. 18: 8. doi: 10.1186/s12900-018-0087-2.

  • Raasakka A.*, Mahootchi E.*, Winge I., Luan W., Kursula P. & Haavik J. (2018) Structure of the mouse acidic amino acid decarboxylase GADL1. Acta Cryst. F74(1): 65-73. doi: 10.1107/S2053230X17017848.


  • Ruskamo S., Nieminen T., Kristiansen C.K., Vatne G.H., Baumann A., Hallin E.I., Raasakka A., Joensuu P., Bergmann U., Vattulainen I. & Kursula P. (2017) Molecular mechanisms of Charcot-Marie-Tooth neuropathy linked to mutations in human myelin protein P2. Sci Rep. 7: 6510. doi: 10.1038/s41598-017-06781-0.

  • Raasakka A., Ruskamo S., Kowal J., Barker R., Baumann A., Martel A., Tuusa J., Myllykoski M., Bürck J., Ulrich A.S., Stahlberg H. & Kursula P. (2017) Membrane Association Landscape of Myelin Basic Protein Portrays Formation of the Myelin Major Dense Line. Sci Rep. 7: 4974. doi: 10.1038/s41598-017-05364-3.

  • Muruganandam G., Raasakka A., Myllykoski M., Kursula I. & Kursula P. (2017) Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase. BMC Biochem. 18: 7. doi: 10.1186/s12858-017-0084-2.

  • Tuusa J., Raasakka A., Ruskamo S. & Kursula P. (2017) Myelin-derived and putative molecular mimic peptides share structural properties in aqueous and membrane-like environments. Mult Scler Demyelinating Disord. 2: 4. doi: 10.1186/s40893-017-0021-7.

  • Snaidero N., Velte C., Myllykoski M., Raasakka A., Ignatev A., Werner H.B., Erwig M.S., Möbius W., Kursula P., Nave K.A. & Simons M. (2017) Antagonistic functions of MBP and CNP establish cytosolic channels in central nervous system myelin. Cell Rep. 18(2): 314-323. doi: 10.1016/j.celrep.2016.12.053.


  • Myllykoski M., Seidel L., Muruganandam G., Raasakka A., Torda A.E. & Kursula P. (2016) Structural and functional evolution of 2’,3’-cyclic nucleotide 3’-phosphodiesterase. Brain Res. 1641(Pt A): 64-78. doi: 10.1016/j.brainres.2015.09.004. Part of the special issue "Evolution of Myelin". Review.


  • Raasakka A., Myllykoski M., Laulumaa S., Lehtimäki M., Härtlein M., Moulin M., Kursula I. & Kursula P. (2015) Determinants of ligand binding and catalytic activity in the myelin enzyme 2′,3′-cyclic nucleotide 3′-phosphodiesterase. Sci Rep. 5: 16520. doi: 10.1038/srep16520.

  • Laulumaa S., Blakeley M.P., Raasakka A., Moulin M., Härtlein M. & Kursula P. (2015) Production, crystallization, and neutron diffraction of fully deuterated human myelin peripheral membrane protein P2. Acta Cryst. F71(11): 1391-1395. doi: 10.1107/S2053230X15017902.

  • Chukhlieb M., Raasakka A., Ruskamo S. & Kursula P. (2015) The N-terminal cytoplasmic domain of neuregulin 1 type III is intrinsically disordered. Amino Acids 47(8): 1567-1577. doi: 10.1007/s00726-015-1998-x.


  • Raasakka A. & Kursula P. (2014) The myelin membrane-associated enzyme 2′,3′-cyclic nucleotide 3′-phosphodiesterase: on a highway to structure and function. Neurosci Bull. 30(6): 956-966. doi: 10.1007/s12264-013-1437-5. Review.


  • Myllykoski M.*, Raasakka A.*, Lehtimäki M., Han H., Kursula I. & Kursula P. (2013) Crystallographic analysis of the reaction cycle of 2’,3’-cyclic nucleotide 3’-phosphodiesterase, a unique member of the 2H phosphoesterase family. J Mol Biol. 425(22): 4307-4322. doi: 10.1016/j.jmb.2013.06.012.


  • Myllykoski M., Raasakka A., Han H. & Kursula P. (2012) Myelin 2’,3’-cyclic nucleotide 3’-phosphodiesterase: Active-site ligand binding and molecular conformation. PLoS ONE 7(2): e32336. doi: 10.1371/journal.pone.0032336.

Conference proceedings

  • Raasakka A., Han H., Myllykoski M. & Kursula P. (2018) Flexibility of the Myelin Scaffolding Protein Periaxin. Biophys J. 114(3): S1,407a. doi: 10.1016/j.bpj.2017.11.2254. (62nd Annual Meeting of the Biophysical Society, San Francisco, CA, 17. - 21.2.2018)

  • Chukhlieb M., Han H., Myllykoski M., Laulumaa S., Raasakka A., Ruskamo S., Wang C. & Kursula P. (2013) Membrane Interactions, Intrinsic Disorder, and Unknown Functions of Myelin Proteins. Biophys J. 104(2): S1,548a. doi: 10.1016/j.bpj.2012.11.3036. (57th Annual Meeting of the Biophysical Society, Philadelphia, PA, 2. - 6.2.2013)


  • Raasakka A. (2019) The Characterization of Disordered Membrane-Binding Proteins of Myelin: A Biophysical Approach. Degree: Philosophiae Doctor (PhD), University of Bergen, Norway. ISBN: 978-82-308-3520-3.

  • Raasakka A. (2012) Structural Enzymology of 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase. Degree: Master of Science (MSc), University of Oulu, Finland.

  • Raasakka A. (2010) TNF-α ja etanersepti - sytokiini ja sen inhibiittori. Degree: Bachelor of Science (BSc), University of Oulu, Finland.

News, highlights and other publications

  • Protein-Lipid Interactions: Advanced Experimental and Computational Tools. Workshop report in NBS Nytt 3/2017: 30-31.


  • Houry D., Raasakka A., Bockwoldt M., Niere M., Heiland I., Kursula P. & Ziegler M. Structural insights into the catalytic mechanism of human NAMPT. The NAD+ Metabolism and Signaling Conference. 23. - 28.6.2019, Dublin, Ireland.

  • Raasakka A., Myllykoski M., Ruskamo S., Baumann A., Kowal J., Stahlberg H., Eichel M., Werner H., Sherman D., Brophy P. & Kursula P. Intrinsic Disorder and Myelin Protein Complexes. Current Topics in Myelin Research. 28.2. - 2.3.2019, Kassel, Germany.

  • Raasakka A., Han H., Myllykoski M. & Kursula P. Flexibility of the Myelin Scaffolding Protein Periaxin. The 62nd Biophysical Society Annual Meeting. 17. - 21.2.2018, San Francisco, CA, United States of America.

  • Raasakka A. & Kursula P. Molecular Flexibility of Myelin Proteins Enables Tight Packing of Lipid Multilayers. The Kavli Prize Symposium in Nanoscience. Atomic Force Microscopy: Yesterday, Today and Tomorrow. 25.9.2017, Zürich, Switzerland.

  • Raasakka A., Baumann A., Barker R., Ruskamo S., Kowal J., Myllykoski M., Bürck J., Stahlberg H. & Kursula P. Myelin Basic Protein - Unraveling Lipid Interactions and Membrane Insertion. 7th Annual BioStruct Conference. 25. - 28.8.2016, Jægtvolden, Norway.

  • Raasakka A., Myllykoski M., Ruskamo S., Laulumaa S. & Kursula P. Exploring the Many Proteins of Myelin - Structural Enzymology and Membrane Stacking in vitro. HERCULES Specialized Course HSC16: Non-atomic resolution scattering in biology and soft matter. 15. - 19.9.2014, Grenoble, France.

  • Raasakka A.*, Laulumaa S.*, Chukhlieb M., Han H., Muruganandam G., Myllykoski M., Ruskamo S. & Kursula P. Structural Biology of the Myelin Membrane - A Biophysical Approach to a Biological Problem. Biocenter Oulu Discovery of the Year. 16.12.2014, Oulu, Finland.


* Equal contribution     † Corresponding author

  • Biophysical and structural characterization of myelin-like proteolipid model systems - The role of protein disorder and net charge in myelination and disease development.
  • Protein-membrane and protein-protein interactions in myelin - Affinity, kinetics, stoichiometry & structure. 

Professional interests

Methods in structural & physical biochemistry, method development & optimization, enzymology, structural biology, neurobiochemistry, teaching


Practical experience

  • Macromolecular X-ray crystallography
  • Small-angle X-ray scattering & diffraction
  • Isotropic & oriented synchrotron circular dichroism spectropolarimetry
  • Synchrotron light sources
  • Neutron reflectometry & small-angle neutron scattering
  • Top-down mass spectrometry; peptide fingerprinting; H-D exchange (MALDI-TOF, LC-ESI-TOF)
  • Atomic force microscopy (mostly imaging)
  • Stopped flow kinetics
  • Surface plasmon resonance (Biacore)
  • Lights scattering methods (SEC-MALS, DLS)
  • UV-vis absorption & fluorescence methods
  • Differential scanning calorimetry
  • Fluorescence-based thermal stability assays (Thermofluor/DSF)
  • Isothermal titration calorimetry
  • Recombinant protein expression using E. coli and S. cerevisiae
  • Protein purification using various chromatography methods
  • Molecular biology methods (classical subcloning & mutagenesis; Gateway cloning)
  • Windows & Linux environments; MS Office; GraphPad Prism; ATSAS; ScÅtter; XDS; Phenix; PyMOL



    • PhD, 2019, Department of Biomedicine, University of Bergen, Norway 
    • MSc, 2012, Department of Biochemistry, University of Oulu, Finland
    • BSc, 2011, Department of Biochemistry, University of Oulu, Finland



    • Department of Biomedicine, University of Bergen, Norway (2015–present)
    • Faculty of Biochemistry and Molecular Medicine (FBMM), University of Oulu, Finland (2013–2015)
    • Centre for Structural Systems Biology, Helmholtz Centre for Infection Research (CSSB-HZI), Hamburg, Germany (2012)
    • Department of Biochemistry, University of Oulu, Finland (2008, 2010–2012)


    Research visits

    • The Integrative Structural Biology lab (ERL 9002 CNRS), University of Lille, France (2019)
    • German Electron Synchrotron (DESY), Hamburg, Germany (2012)

    Research groups