Finnish Biological NMR Center

The mission of the Finnish Biological NMR Center is to carry out academic research dedicated to improving the understanding of biomolecules, and provide quality services in the field of NMR spectrometry.

We offer access to state-of-the-art equipment and the expertise of our staff to further your research.

Instruct-ERIC Centre Finland / NMR

NMR services are part of Instruct-ERIC Centre Finland and can be accessed also through Instruct-ERIC (Instruct Centre Finland / NMR service home pages). See funding possibilities for Instruct-ERIC access.

NMR Services
  • Basic and advanced NMR services
NMR applications

Our High-field NMR instruments are perfect non-destructive tool to e.g.:

  • Determine structure of a macromolecule in liquid state
  • Study protein-ligand and protein-protein interactions in liquid state
  • Characterise dynamics of a macromolecule over a wide range of time scales
  • Determine protein size with Diffusion spectroscopy
  • Analyse protein backbone dynamics
  • Study effects of a mutation to structure
  • 1H, 13C and 15N NMR
  • 19F NMR
  • 29Si NMR
  • 31P NMR
  • Small molecule NMR
NMR instrumentation

850 MHz Avance III HD

600 MHz Avance III

600 MHz Avance III (VTT)

  • Equipped with Cryogenically cooled QCI 1H-13C/31P/15N/D probehead
NMR Sample requirements

NMR sample should be soluble to NMR solvents and contain no solid particles.

The buffer should not contain any other small molecules (eg. HEPES, TRIS, EDTA).

Salt concentration should be as low as possible, <100 mM.

  • Preferred solvents
    • 5% D2O:H2O for protein samples
    • D2O, CDCl3, DMSO-D6, Acetone-D6
  • Minimum Volume
    • 500 µl for 5 mm tube
    • 250 µl for 5mm Shigemi tube
  • Minimum Concentrations
    • 0.05 mM for 1H experiment
    • 0.1 mM for 2D experiments
    • 0.1 - 0.3 mM  for protein NMR

NMR user policy
  • NMR Core facility is open to both academic and commercial users.
  • To start a project
    •  register and login to Ilab
      • Send project request
    • or contact grp-nmrservice[at]
  • Acknowledgements: User agrees to acknowledge the NMR center in the upcoming publications and theses with e.g. the following text:

    "The facilities and expertise of the HiLIFE NMR unit at the University of Helsinki, a member of Instruct-ERIC Centre Finland, FINStruct, and Biocenter Finland are gratefully acknowledged."
  • Users agree to send the bibliography of the published material (scientific papers, theses) to grp-nmrservice[at]
  • Old Reservation book (not in use 6.2.2023->)
NMR Pricelist

From 15.2.2023 onwards

850 MHz Spectrometer time €/Hour €/Day €/Week*
Internal (UH) 20 210 1050
BF 25 260 1300
External 342 ** **

* 7 consecutive days

**Ask for quotation

600 MHz Spectrometer time €/Hour €/Day €/Week*
Internal (UH) 7 73 365
BF 9 95 475
External 291 ** **

* 7 consecutive days

**Ask for quotation

Operator time €/hour
Internal & BF 23


NMR publications


  • Dryś, M., Koso, T.V., Kilpeläinen, P.O., Rinne-Garmston, K.T., Todorov, A.R., Wiedmer, S.K., Iashin, V., King, A.W.T. (2024) Structural Characterization of 6-Halo-6-Deoxycelluloses by Direct-Dissolution Solution-State NMR Spectroscopy. Macromolecular rapid communications, e2300698. Advance online publication. DOI:10.1002/marc.202300698
  • Nencini, R., Regnier, M.L.G., Backlund, S.M., Mantzari, E., Dunn, C.D., Ollila, O.H.S. (2024) Probing the dynamic landscape of peptides in molecular assemblies by synergized NMR experiments and MD simulations. Communications chemistry, 7(1), 28. DOI:10.1038/s42004-024-01115-4
  • Iwaï, H., Beyer, H.M., Johansson, J.E.M., Li, M., Wlodawer, A. (2024). The three-dimensional structure of the Vint domain from Tetrahymena thermophila suggests a ligand-regulated cleavage mechanism by the HINT fold. FEBS letters, Advance online publication. DOI:10.1002/1873-3468.14817
  • Klukowski, P., Damberger, F.F., Allain, F.H., Iwai, H., Kadavath, H., Ramelot, T.A., Montelione, G.T., Riek, R., Güntert, P. (2024) The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis. Scientific data, 11(1), 30. DOI:10.1038/s41597-023-02879-5


  • Holler, C.V., Petersson, N.M., Brohus, M., Niemelä, M.A., Iversen, E.D., Overgaard, M.T., Iwaï, H., & Wimmer, R. (2023). Allosteric changes in protein stability and dynamics as pathogenic mechanism for calmodulin variants not affecting Ca2+ coordinating residues. Cell calcium, 117, 102831. Advance online publication. DOI:10.1016/j.ceca.2023.102831
  • Akbari, S., Root, A., Skrifvars, M., Ramamoorthy, S.K., Åkesson, D. (2023). Novel Bio-based Branched Unsaturated Polyester Resins for High-Temperature Applications. J Polym Environ (2023). DOI: 10.1007/s10924-023-03112-5
  • Lahtinen, M.H., Kynkäänniemi, E., Jian, C., Salonen, A., Pajari, A.M., & Mikkonen, K.S. (2023). Metabolic Fate of Lignin in Birch Glucuronoxylan Extracts as Dietary Fiber Studied in a Rat Model. Molecular nutrition & food research, e2300201. Advance online publication. DOI:10.1002/mnfr.202300201
  • Xia, J., Koso, T., Heise, K., Fliri, L., Ressouche, E., Majoinen, J., Kostiainen, M.A., Hietala, S., Hummel, M., Aseyev, V., Kilpeläinen, I., & King, A.W.T. (2023). Stable glycosylamines at the reducing ends of cellulose nanocrystals. Chemical communications (Cambridge, England), 59(61), 9408–9411. DOI:10.1039/d3cc01329d
  • Moliner, R., Girych, M., Brunello, C.A., Kovaleva, V., Biojone, C., Enkavi, G., Antenucci, L., Kot, E.F., Goncharuk, S. A., Kaurinkoski, K., Kuutti, M., Fred, S.M., Elsilä, L.V., Sakson, S., Cannarozzo, C., Diniz, C.R.A.F., Seiffert, N., Rubiolo, A., Haapaniemi, H., Meshi, E., Nagaeva, E., Öhman, T., Róg, T., Kankuri, E., Vilar, M., Varjosalo, M., Korpi, E.R., Permi, P., Mineev, K.S., Saarma, M., Vattulainen, I., Casarotto, P.C., Castrén, E. (2023). Psychedelics promote plasticity by directly binding to BDNF receptor TrkB. Nat Neurosci. 2023 Jun;26(6):1032-1041. DOI:10.1038/s41593-023-01316-5
  • Fliri, L., Heise, K., Koso, T., Todorov, A. R., Del Cerro, D.R., Hietala, S., Fiskari, J., Kilpeläinen, I., Hummel, M., & King, A.W.T. (2023). Solution-state nuclear magnetic resonance spectroscopy of crystalline cellulosic materials using a direct dissolution ionic liquid electrolyte. Nature protocols, 18(7), 2084–2123. DOI:10.1038/s41596-023-00832-9


  • Haider, M.S., Mahato, A.K., Kotliarova, A., Forster, S., Böttcher, B., Stahlhut, P., Sidorova, Y., Luxenhofer, R. (2022). Biological Activity In Vitro, Absorption, BBB Penetration, and Tolerability of Nanoformulation of BT44:RET Agonist with Disease-Modifying Potential for the Treatment of Neurodegeneration. Biomacromolecules. Doi:10.1021/acs.biomac.2c00761
  • Beyer, H.M., Iwaï, H. (2022). Propagation of Homing Endonuclease-Associated Inteins. Front Mol Biosci. 2022 Mar 16;9:855511. DOI:10.3389/fmolb.2022.855511
  • Heikkinen, H. A., Aranko, A. S., & Iwaï, H. (2022). The NMR structure of the engineered halophilic DnaE intein for segmental isotopic labeling using conditional protein splicing. Journal of magnetic resonance, 338, 107195. DOI:10.1016/j.jmr.2022.107195


  • Sokka, I.K., Imlimthan, S., Sarparanta, M., Maaheimo, H., Johansson, M.P., Ekholm, F.S. (2021). Halogenation at the Phenylalanine Residue of Monomethyl Auristatin F Leads to a Favorable cis/trans Equilibrium and Retained Cytotoxicity. Molecular Pharmaceutics 2021 18 (8), 3125-3131 Doi:10.1021/acs.molpharmaceut.1c00342
  • de Carvalho, D.M., Lahtinen, M.H., Bhattarai, M., Lawoko, M., Mikkonen, K.S. (2021) Active role of lignin in anchoring wood-based stabilizers to the emulsion interface. Green Chem., 2021,23, 9084-9098. DOI:10.1039/D1GC02891J
  • Renko, J.M., Mahato, A.K., Visnapuu, T., Valkonen, K., Karelson, M., Voutilainen, M.H., Saarma, M., Tuominen, R.K., & Sidorova, Y.A. (2021) Neuroprotective Potential of a Small Molecule RET Agonist in Cultured Dopamine Neurons and Hemiparkinsonian Rats. Journal of Parkinson's disease, 11(3), 1023–1046. DOI:10.3233/JPD-202400
  • Figueiredo, P., Lahtinen, M.H., Agustin, M.B., de Carvalho, D.M., Hirvonen, S.-P., Penttilä, P.A. and Mikkonen, K.S. (2021) Green Fabrication Approaches of Lignin Nanoparticles from Different Technical Lignins: A Comparison Study. ChemSusChem. DOI:10.1002/cssc.202101356
  • Mattila, A.L.K., Jiggins, C.D., Opedal, Ø.H., Montejo-Kovacevich, G., de Castro, É., McMillan, W.O., Bacquet, C., Saastamoinen, M. (2021) Evolutionary and ecological processes influencing chemical defense variation in an aposematic and mimetic Heliconius butterfly. PeerJ. 2021 Jun 18;9:e11523. doi: 10.7717/peerj.11523
  • Aranko, A.S., Iwaï, H. (2021) The Inducible Intein-Mediated Self-Cleaving Tag (IIST) System: A Novel Purification and Amidation System for Peptides and Proteins. Molecules. 2021; 26(19):5948. DOI:10.3390/molecules26195948
  • Heikkinen, H.A., Backlund, S.M., Iwaï, H. (2021) NMR Structure Determinations of Small Proteins Using only One Fractionally 20% 13C- and Uniformly 100% 15N-Labeled Sample. Molecules. 2021; 26(3):747.
  • Hsu, S.D., Lee, Y.C., Mikula, K.M., Backlund, S.M., Tascón, I., Goldman, A., & Iwaï, H. (2021) Tying up the Loose Ends: A Mathematically Knotted Protein. Frontiers in chemistry, 9, 663241. DOI:10.3389/fchem.2021.663241 
  • Hiltunen, M.K., Beyer, H.M., Iwaï, H. (2021) Mini-Intein Structures from Extremophiles Suggest a Strategy for Finding Novel Robust Inteins. Microorganisms 2021, 9, 1226.
  • Eesmaa, A., Yu, L.Y., Göös, H., Nõges, K., Kovaleva, V., Hellman, M., Zimmermann, R., Jung, M., Permi, P., Varjosalo, M., Lindholm, P., Saarma, M. (2021) The cytoprotective protein MANF promotes neuronal survival independently from its role as a GRP78 cofactor. J Biol Chem. 2021 Jan-Jun;296:100295. DOI: 10.1016/j.jbc.2021.100295.


  • Viisanen, H., Nuotio, U., Kambur, O., Mahato, A.K., Jokinen, V., Lilius, T., Li, W., Santos, H.A., Karelson, M., Rauhala, P., Kalso, E., & Sidorova, Y.A. (2020). Novel RET agonist for the treatment of experimental neuropathies. Molecular Pain. January 2020. DOI: 10.1177/1744806920950866
  • Duplouy, A., Minard, G., Saastamoinen, M. (2020). The gut bacterial community affects immunity but not metabolism in a specialist herbivorous butterfly. Ecol Evol. 2020; 10: 8755– 8769.
  • Carvalho, D.M.D., Lahtinen, M.H., Lawoko, M., Mikkonen, K.S. (2020), Enrichment and Identification of Lignin–Carbohydrate Complexes in Softwood Extract, ACS Sustainable Chem. Eng. 2020, 8, 31, 11795–11804, DOI:10.1021/acssuschemeng.0c03988
  • Beyer, H.M., Virtanen, S.I., Aranko, A.S., Mikula, K.M., Lountos, G.T., Wlodawer, A., Ollila, O.H.S., Iwaï, H. (2020), The Convergence of the Hedgehog/Intein Fold in Different Protein Splicing Mechanisms,  Int J Mol Sci. 2020 Nov 7;21(21):8367, DOI:10.3390/ijms21218367 
  • Virtanen, S.I., Kiirikki, A.M., Mikula, K.M., Iwaï, H., Ollila, O.H.S. (2020), Heterogeneous dynamics in partially disordered proteins, Phys. Chem. Chem. Phys., 2020,22, 21185-21196, DOI:10.1039/d0cp03473h
  • Oeemig, J.S., Beyer, H.M., Aranko, A.S., Mutanen, J., Iwaï, H. (2020), Substrate specificities of inteins investigated by QuickDrop-cassette mutagenesis, FEBS Lett. 2020 Aug 17, DOI:10.1002/1873-3468.13909.
  • Jaakkonen, A., Volkmann, G., Iwaï, H. (2020), An Off-the-Shelf Approach for the Production of Fc Fusion Proteins by Protein Trans-Splicing towards Generating a Lectibody In Vitro, Int. J. Mol. Sci. 2020, 21(11), 4011, DOI:10.3390/ijms21114011.
  • Ciragan, A., Backlund, S.M., Mikula, K.M., Beyer, H.M., Ollila, O.H.S., Iwaï, H. (2020) NMR Structure and Dynamics of TonB Investigated by Scar-Less Segmental Isotopic Labeling Using a Salt-Inducible Split Intein. Front. Chem., 19 March 2020, DOI: 10.3389/fchem.2020.00136
  • Mahato, A.K., Kopra, J., Renko, J.‐M., Visnapuu, T., Korhonen, I., Pulkkinen, N., Bespalov, M.M., Domanskyi, A., Ronken, E., Piepponen, T.P., Voutilainen, M.H., Tuominen, R.K., Karelson, M., Sidorova, Y.A. and Saarma, M. (2020), Glial cell line–derived neurotrophic factor receptor Rearranged during transfection agonist supports dopamine neurons in Vitro and enhances dopamine release In Vivo. Mov Disord, 35: 245-255. doi:10.1002/mds.27943


  • Beyer, H.M., Mikula, K.M., Li, M., Wlodawer, A., Iwaï, H. (2019) The crystal structure of the naturally split gp41-1 intein guides the engineering of orthogonal split inteins from cis-splicing inteins. FEBS J. 2019 Oct 30, DOI: 10.1111/febs.15113
  • Beyer, H.M., Iwaï, H. (2019) Off-Pathway-Sensitive Protein-Splicing Screening Based on a Toxin/Antitoxin System. Chembiochem. 2019 Aug 1;20(15):1933-1938. DOI: 10.1002/cbic.201900139
  • Minard, G., Tikhonov, G., Ovaskainen, O., Saastamoinen, M. (2019) The microbiome of the Melitaea cinxia butterfly shows marked variation but is only little explained by the traits of the butterfly or its host plant. Environ Microbiol, 21: 4253-4269. doi:10.1111/1462-2920.14786
  • Mollerup, F., Aumala, V., Parikka, K., Mathieu, Y., Brumer, H., Tenkanen, M., Master, E. (2019) A family AA5_2 carbohydrate oxidase from Penicillium rubens displays functional overlap across the AA5 family. PLOS ONE 14(5): e0216546.
  • Agustin, M.B., Penttilä, P.A., Lahtinen, M., Mikkonen, K.S. (2019) Rapid and Direct Preparation of Lignin Nanoparticles from Alkaline Pulping Liquor by Mild Ultrasonication, ACS Sustainable Chem. Eng. 2019, DOI: 10.1021/acssuschemeng.9b05445
  • Mattila, A., Andsten, R.M., Jumppanen, M., Assante, M., Jokela, J., Wahlsten, M., Mikula, K.M., Sigindere, C., Kwak, D.H., Gugger, M., Koskela, H., Sivonen, K., Liu, X., Yli-Kauhaluoma, J., Iwai, H., Fewer, D.P. (2019) Biosynthesis of the bis-prenylated alkaloids muscoride A and B. ACS Chem. Biol., DOI: 10.1021/acschembio.9b00620
  • Valoppi, F., Lahtinen, M.H., Bhattarai, M., Kirjoranta, S.J., Juntti, V.K., Peltonen, L.J., Kilpeläinen, P.O., Mikkonen, K.S. (2019) Centrifugal fractionation of softwood extracts improves the biorefinery workflow and yields functional emulsifiers. Green Chem. vol 21 4691-4705, DOI: 10.1039/c9gc02007a
  • Beyer, H.M., Mikula, K.M., Kudling, T.V., Iwai, H. (2019) Crystal structures of CDC21-1 inteins from hyperthermophilic archaea reveal the selection mechanism for the highly conserved homing endonuclease insertion site, Extremophiles 23: 669. DOI: 10.1007/s00792-019-01117-4


  • Shiraishi, Y., Natsume, M., Kofuku, Y., Imai, S., Nakata, K., Mizukoshi, T., Ueda, T., Iwaï, H. & Shimada, I. (2018) Phosphorylation-induced conformation of β2-adrenoceptor related to arrestin recruitment revealed by NMR, Nat. Commun. 9:194. DOI: 10.1038/s41467-017-02632-8
  • Oeemig, J.S., Ollila, O.H.S., Iwaï, H. (2018) NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa, PeerJ 6:e5412, DOI: 10.7717/peerj.5412
  • Ollila, O.H.S, Heikkinen, H.A., Iwai, H. (2018) Rotational Dynamics of Proteins from Spin Relaxation Times and Molecular Dynamics Simulations, J. Phys. Chem. B. 122, 25. DOI: 10.1021/acs.jpcb.8b02250
  • Tossavainen, H., Raulinaitis, V., Kauppinen, L., Pentikäinen, U., Maaheimo, H., Permi, P. (2018) Structural and Functional Insights Into Lysostaphin–Substrate Interaction, Front Mol Biosci. 2018; 5: 60. DOI: 10.3389/fmolb.2018.00060
  • King, A.W.T., Mäkelä, V., Kedzior, S.A., Laaksonen, T., Partl, G.J., Heikkinen, S., Koskela, H., Heikkinen, H.A., Holding, A.J., Cranston, E.D., Kilpeläinen, I. (2018) Liquid-State NMR Analysis of Nanocelluloses, Biomacromolecules, DOI: 10.1021/acs.biomac.8b00295
  • Mikula, K.M., Krumwiede, L., Plückthun, A., Iwai, H. (2018) Segmental isotopic labeling by asparaginyl endopeptidase-mediated protein ligation, J Biomol NMR Doi:10.1007/s10858-018-0175-4
  • Norppa, A.J., Kauppala, T.M., Heikkinen, H.A., Verma, B., Iwaï, H. & Frilander, M.J. (2018) Mutations in the U11/U12-65K protein associated with isolated growth hormone deficiency lead to structural destabilization and impaired binding of U12 snRNA. RNA in press doi: 10.1261/rna.062844.117.


  • Johansson, M. P., Maaheimo, H., & Ekholm, F. S. (2017). New insight on the structural features of the cytotoxic auristatins MMAE and MMAF revealed by combined NMR spectroscopy and quantum chemical modelling. Scientific reports, 7(1), 15920.
  • Minato, Y., Ueda, T., Machiyama, A., Iwaï, H. & Shimada, I. (2017) Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR, Sci Rep. 2017 Nov 28;7(1):16462. DOI: 10.1038/s41598-017-16755-x
  • Iwaï. H., Mikula, K.M., Oeemig, J.S., Zhou,D. Li, M., & Wlodawer, A. (2017) Structural basis for the persistence of homing endonucleases in transcription factor IIB inteins. J. Mol. Biol. 429, 3942–3956. doi:10.1016/j.jmb.2017.10.016
  • Otrusinová. O., Demo, G., Padrta, P., Jaseňáková, Z., Pekárová, B., Gelová, Z., Szmitkowska, A., Kadeřávek, P., Jansen, S., Zachrdla, M., Klumpler, T., Marek, J., Hritz, J., Janda, L., Iwaï, H., Wimmerová, M., Hejátko, J., Žídek, L. (2017) Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase from Arabidopsis thaliana. J Biol Chem. 2017 Oct 20;292(42):17525-17540. DOI: 10.1074/jbc.M117.790212
  • Raulinaitis, V., Tossavainen, H., Aitio, O., Juuti, J.T., Hiramatsu, K., Kontinen, V., Permi, P. (2017) Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family. Scientific Reports 7, Article number: 6020. doi:10.1038/s41598-017-06135-w
  • Mikula, K. M., Tascón, I., Tommila, J. J., Iwaï, H. (2017) Segmental isotopic labeling of a single-domain globular protein without any refolding step by an asparaginyl endopeptidase. FEBS Lett. 591: 1285–1294. doi:10.1002/1873-3468.12640
  • Ahlstrand, T., Tuominen, H., Beklen, A., Torittu, A., Oscarsson, J., Sormunen, R., Pöllänen, M. T., Permi, P., Ihalin, R. (2017) A novel intrinsically disordered outer membrane lipoprotein of Aggregatibacter actinomycetemcomitans binds various cytokines and plays a role in biofilm response to interleukin-1β and interleukin-8. Virulence 2017; 8(2): 115-134; PMID:27459270; doi: 10.1080/21505594.2016.1216294
  • Raulinaitis, V., Tossavainen, H., Aitio, O., Seppälä, R., Permi, P. (2017) 1H, 13C and 15N resonance assignments of the new lysostaphin family endopeptidase catalytic domain from Staphylococcus aureus.  Biomol NMR Assign 11: 69. doi:10.1007/s12104-016-9722-7


  • Ciragan, A., Aranko, A. S., Tascon, I., Iwaï, H. (2016) Salt-inducible protein splicing in cis and trans by inteins from extremely halophilic archaea as a novel protein-engineering tool. J. Mol. Bio 428, 4573-4588.
  • Jin, C., Viidanoja, J., Li, M., Zhang, Y., Ikonen, E., Root, A., Romanczyk, M., Manheim, J., Dziekonski, E., Kenttämaa, H. I. (2016) Comparison of Atmospheric Pressure Chemical Ionization and Field Ionization Mass Spectrometry for the Analysis of Large Saturated Hydrocarbons. Anal. Chem. 88 (21), 10592-10598. DOI: 10.1021/acs.analchem.6b02789
  • Laitaoja, M., Tossavainen, H., Pihlajamaa, T., Valjakka, J., Viiri, K., Lohi, O., Permi, P., Jänis, J. (2016), Redox-dependent disulfide bond formation in SAP30L corepressor protein: Implications for structure and function. Protein Sci, 25: 572–586
  • Tossavainen, H., Aitio, O., Hellman, M., Saksela, K., Permi, P. ( 2016) Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2. J. Biol. Chem. 291, 16307– 16317, DOI: 10.1074/jbc.M116.732412
  • Harju, K., Koskela, H., Kremp, A., Suikkanen, S., de la Iglesia, P., Miles, C. O., Krock, B., Vanninen, P. (2016) Identification of gymnodimine D and presence of gymnodimine variants in the dinoflagellate Alexandrium ostenfeldii from the Baltic Sea. Toxicon, 112 pp. 68–76


  • Vegh, R. B., Bloch, D. A., Bommarius, A. S., Verkhovsky, M., Pletnev, S., Iwaï, H., Bochenkova, A. V., Solntsev, K. M. (2015) Hidden Photoinduced Reactivity of the Blue Fluorescent Protein mKalama1. Phys. Chem. Chem. Phys., 17(19):12472-12485. DOI: 10.1039/c5cp00887e
  • Guerrero, F., Ciragan, A., Iwaï, H. (2015) Tandem SUMO fusion vectors for improving soluble protein expression and purification. Protein Expression Purif. 116, 42–49.
  • Tossavainen, H., Seppälä, J., Sethi, R., Pihlajamaa, T., Permi, P. (2015) HN, NH, Cα, Cβ, and methyl group assignments of filamin multidomain fragments IgFLNc4–5 and IgFLNa3–5. Biomol NMR Assign 9: 47. doi:10.1007/s12104-014-9542-6
  • Piirainen H., Hellman M., Tossavainen H., Permi P., Kursula P. and Jaakola V. P. (2015) Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. Biophys. J. 108, 903–917. DOI: 10.1016/j.bpj.2014.12.036
  • Liu, L., Budnjo, A., Jokela, J., Haug, B. E., Fewer, D. P, Wahlsten, M., Rouhiainen, L., Permi, P., Fossen, T., Sivonen, K. (2015) Pseudoaeruginosins, Nonribosomal Peptides in Nodularia spumigena. ACS Chem. Biol. 10 (3), 725-733. DOI: 10.1021/cb5004306
  • Shishido, T. K., Humisto, A., Jokela, J., Liu, L., Wahlsten, M., Tamrakar, A., Fewer, D. P., Permi, P., Andreote, A. P. D., Fiore, M. F., Sivonen, K. (2015) Antifungal Compounds from Cyanobacteria. Mar. Drugs 13, 2124-2140. DOI:10.3390/md13042124
  • Tossavainen, H., Hellman, M., Piirainen, H. Jaakola, V. P., Permi, P. (2015) HN, N, Cα, Cβ and C′ assignments of the intrinsically disordered C-terminus of human adenosine A2A receptor. Biomol NMR Assign 9: 403. doi:10.1007/s12104-015-9618-y
  • Seppälä, J., Tossavainen, H., Rodic, N., Permi, P., Pentikäinen, U., Ylänne, J. (2015). Flexible structure of peptide-bound filamin A mechanosensor domain pair 20-21. PLoS One, 10(8) doi:
  • Martikainen, M., Salorinne, K., Lahtinen, T., Malola, S., Permi, P., Häkkinen, H., Marjomaki, V. (2015) Hydrophobic Pocket Targeting Probes for Enteroviruses. Nanoscale 7, 17457– 17467, DOI: 10.1039/C5NR04139B


  • Aranko, A. S., Oeemig, J. S., Zhou, D., Kajander, T., Wlodawer, A., Iwaï, H. (2014) Structure-based engineering and comparison of novel split inteins for protein ligation. Mol. Biosyst. 10 (5), 1023 - 1034 DOI: 10.1039/c4mb00021h
  • Aranko, A. S., Wlodawer, A., Iwaï, H. (2014) Nature’s recipe for splitting inteins. Protein Eng. Des. Sel. 27(8), 263–271. DOI:10.1093/protein/gzu028
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