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


  • 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

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)
    • 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. 

    Research groups