Finnish Biological NMR Center

  • Basic and advanced NMR services

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
  • 19F measurements
  • Small molecule NMR
  • NMR Core facility is open to both academic and commercial users.
  • Customers are served based on reservations made in the Reservation book
  • Please contact grp-nmrservice[at] to start a project

Updated 23.8.2019

UH/BF user
(University of Helsinki and Biocenter Finland)

Spectrometer time WITH OPERATOR
  Charges €/h
  1st & 2nd hour 3rd to 6th hour 7th hour onwards
850 MHz TCI CryoProbe 235 €/h 120 €/h 10 €/h
600 MHz BB SmartProbe 40 €/h 20 €/h 3 €/h
600 MHz TCI CryoProbe 80 €/h 40 €/h 6 €/h
Spectrometer time WITHOUT OPERATOR
850 MHz TCI CryoProbe 10 €/h    
600 MHz BB SmartProbe 3 €/h    
600 MHz TCI CryoProbe 6 €/h    

Academic user (non UH/BF)

Spectrometer time WITH OPERATOR
  Charges €/h
  1st & 2nd hour 3rd to 6th hour 7th hour onwards
850 MHz TCI CryoProbe 250 €/h 150 €/h 55 €/h
600 MHz BB SmartProbe 60 €/h 30 €/h 10 €/h
600 MHz TCI CryoProbe 100 €/h 50 €/h 15 €/h
Spectrometer time WITHOUT OPERATOR
850 MHz TCI CryoProbe 55 €/h    
600 MHz BB SmartProbe 10 €/h    
600 MHz TCI CryoProbe 15 €/h    

Non-academic user

Spectrometer time WITH OPERATOR
  Charges €/h
  1st & 2nd hour 3rd to 6th hour 7th hour onwards
850 MHz TCI CryoProbe 310 €/h 260 €/h 235 €/h
600 MHz BB SmartProbe 100 €/h 70 €/h 40 €/h
600 MHz TCI CryoProbe 150 €/h 90 €/h 60 €/h
Spectrometer time WITHOUT OPERATOR
850 MHz TCI CryoProbe 235 €/h    
600 MHz BB SmartProbe 40 €/h    
600 MHz TCI CryoProbe 60 €/h    


NMR tubes Academic (Non-academic)
5 mm, normal 2 € (3 €)
3 mm, normal 17 € (20 €)
5 mm, shigemi 100 € (115 €)
4 mm, shigemi 100 € (115 €)
3 mm, shigemi 100 € (115 €)
Solvents €/sample
D2O 1 €/sample (1 €/sample)
DMSO-D6 3 €/sample (4 €/sample)
CDCl3 1 €/sample (1 €/sample)
MeOD-D4 9 €/sample (10 €/sample)
Acetone-D6 4 €/sample (5 €/sample)
Prices for other solvents on request  



  • 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, DOI: 10.1007/s00792-019-01117-4

  • 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. DOI: 10.1021/acs.jpcb.8b02250

  • 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.


  • 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

  • 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
  • Shunmugam, S., Jokela, J., Wahlsten, M., Battchikova, N., Rehman, A. U., Vass, I., Karonen, M., Sinkkonen, J., Permi, P., Sivonen, K., Aro, E.-M., Allahverdiyeva, Y. (2014) Secondary metabolite from Nostoc XPORK14A inhibits photosynthesis and growth of Synechocystis PCC 6803. Plant Cell Environ. 37: 1371–1381. doi:10.1111/pce.12243
  • Hellman, M., Piirainen, H., Jaakola, V. P., Permi, P. (2014) Bridge over troubled proline: assignment of intrinsically disordered proteins using (HCA)CON(CAN)H and (HCA)N(CA)CO(N)H experiments concomitantly with HNCO and i(HCA)CO(CA)NH. J. Biomol. NMR 58: 49. doi:10.1007/s10858-013-9804-0
  • Sethi, R., Seppälä, J., Tossavainen, H., Ylilauri, M., Ruskamo, S., Pentikäinen, O. T., Pentikäinen, U., Permi, P., Ylänne, J. (2014) A Novel Structural Unit in the N-terminal Region of Filamins. J. Biol. Chem. 289: 8588–98. pmid:24469451 DOI: 10.1074/jbc.M113.537456 
  • Vestola, J., Shishido T. K., Jokela, J., Fewer, D. P., Aitio, O., Permi, P., Wahlsten, M., Wang, H., Rouhiainen, L., Sivonen, K. (2014) Hassallidins, antifungal glycolipopeptides, are widespread among cyanobacteria and are the end-product of a nonribosomal pathway. PNAS 111 (18) E1909-E1917, doi:10.1073/pnas.1320913111 
  • Tossavainen, H., Kukkurainen, S., Määttä, J. A. E., Kähkönen, N., Pihlajamaa, T., Hytönen, V. P., Kulomaa, M. S., Permi, P. (2014) Chimeric Avidin – NMR Structure and Dynamics of a 56 kDa Homotetrameric Thermostable Protein. PLoS ONE 9(6): e100564.
  • Liu, L., Jokela, J., Wahlsten, M., Nowruzi, B., Permi, P., Zhang, Y. Z., Xhaard, H., Fewer D.P., Sivonen K. (2014) Nostosins, Trypsin Inhibitors Isolated from the Terrestrial Cyanobacterium Nostoc sp. Strain FSN. J. Nat. Prod. 77 (8), 1784-1790 DOI: 10.1021/np500106w
  • Liu, L., Jokela, J., Herfindal, L., Wahlsten, M., Sinkkonen, J., Permi, P., Fewer, D. P., Døskeland, S. O., Sivonen, K. (2014) 4-Methylproline Guided Natural Product Discovery: Co-Occurrence of 4-Hydroxy- and 4-Methylprolines in Nostoweipeptins and Nostopeptolides. ACS Chem. Biol. 9 (11), 2646-2655 DOI: 10.1021/cb500436p


  • Aranko, A. S., Oeemig, J. S., Iwaï, H. (2013) Structural basis for protein trans-splicing by a Bacterial Intein-Like domain: protein ligation without nucleophilic side-chains. FEBS J. 280, 3256-3269 
  • Bhattacharjee, A., Oeemig, J. S., Kolodziejczyk, R., Meri, T., Kajander, T., Iwaï, H., Jokiranta, T. S., Goldman, A. (2013) Structural basis for complement evasion by Lyme disease pathogen Borrelia burgdorferi. J. Biol. Chem. 288, 18685-18695
  • Aranko, A. S., Oeemig, J. S., Kajander, T., Iwaï H. (2013) Intermolecular domain swapping induces intein-mediated protein alternative splicing. Nat. Chem. Biol. 9, 616–622
  • Pihlajamaa, T., Kajander, T., Knuuti, J., Horkka, K., Sharma, A., Permi, P. (2013) Structure of Plasmodium falciparum TRAP (thrombospondin-related anonymous protein) A domain highlights distinct features in apicomplexan von Willebrand factor A homologues. Biochemical J.  450 (3) 469-476; DOI: 10.1042/BJ20121058 
  • Tossavainen, H., Helppolainen, S. H., Määttä, J. A. E., Pihlajamaa, T., Hytönen, V. P., Kulomaa, M. S., Permi, P. (2013) Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms. Biomol NMR Assign 7: 35. doi:10.1007/s12104-012-9371-4
  • Leikoski, N., Liu, L., Jokela, J., Wahlsten, M., Gugger, M., Calteau, A., Permi, P., Kerfeld, C. A., Sivonen, K., Fewer, D. P. (2013) Genome mining expands the chemical diversity of the cyanobactin family to include highly modified linear peptides. Chem Biol 2013, 1033–1043, doi: 10.1016/j.chembiol.2013.06.015
  • Fewer, D. P., Jokela, J., Paukku, E., Österholm, J., Wahlsten, M., Permi, P., Aitio, O., Rouhiainen, L., Gomez-Saez, G. V., Sivonen, K. (2013) New Structural Variants of Aeruginosin Produced by the Toxic Bloom Forming Cyanobacterium Nodularia spumigena. PLoS ONE 8(9): e73618. doi: 10.1371/journal.pone.0073618