Wiktor Koźmiński's NMR group

Biological and Chemical Research Centre, University of Warsaw

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Publications since 2005:

  1. A novel high-dimensional NMR experiment for resolving protein backbone dihedral angle ambiguities, C. Kauffmann, K. Kazimierczuk, T. C. Schwarz, R. Konrat, A. Zawadzka-Kazimierczuk, J. Biomol. NMR, 74, 257-265, (2020).
  2. Automated Backbone NMR Resonance Assignment of Large Proteins Using Redundant Linking from a Single Simultaneous Acquisition, J. Stanek, T. Schubeis, P. Paluch, P. Günter, L. B. Andreas, G. Pintacuda, J. Am. Chem. Soc., 142, 5793-5799, (2020).
  3. Metal exchange in interprotein Zn(II)‐binding site of Rad50 hook domain – structural insights into Cd(II)‐induced DNA repair inhibition, M. Padjasek, M. Maciejczyk, M. Nowakowski, O. Kerber, M. Pyrka, W. Koźmiński, A. Krężel,  Chem. Eur. J., 23, 3297-3313, (2019).
  4. Protein NMR resonance assignment without spectral analysis: 5D SOlid‐state Automated Projection SpectroscopY (SO‐APSY), H. W. Orton, J. Stanek, T. Schubeis, D. Foucaudeau, C. Ollier, A. W. Draney, T. Le Marchand, D. Cala-De Paepe, I. C. Felli, R. Pierattelli, S. Hiller, W. Bermel, G. Pintacuda,  Angew. Chem. Int. Ed., 132, 2400-2405, (2019).
  5. Towards the functional high-resolution coordination chemistry of blood plasma human serum albumin, S. Al-Harthi, J. Lachowicz, M. Nowakowski, M. Jaremko, Ł. Jaremko,  J. Inorg. Biochem., 198, 110716, (2019).
  6. Novel Cyclic Biphalin Analogues by Ruthenium-Catalyzed Ring Closing Metathesis: in Vivo and in Vitro Biological Profile, A. Stefanucci, W. Lei, S. Pieretti, M. Pia Dimmito, G. Luisi, E. Novellino, M. Nowakowski, W. Koźmiński, S. Mirzaie, G. Zengin, J. M. Streicher, A. Mollica,  ACS Med. Chem. Lett., 10, 450-456, (2019).
  7. Shape adaptation of quinine in cyclodextrin cavities: NMR studies, J. Wójcik, A. Ejchart, M. Nowakowski,  Phys. Chem. Chem. Phys., 21, 6925-6934, (2019).
  8. Structural analysis of 25-hydroxycholesterol stereoisomers differing in configuration in position 17 and 20, by three-dimensional NMR spectra, M. Misiak, W. Koźmiński, J. Wójcik, R. R. Siciński, J. Wicha,  Steroids, 143, 49-52, (2019).
  9. 19F multiple-quantum coherence NMR spectroscopy for probing protein–ligand interactionsng protein–ligand interactions, A. Zawadzka-Kazimierczuk, M. Somlyay, H. Kaehlig, G. Iakobson, P. Beierd, R. Konrat,  RSC Adv., 8, 40687-40692, (2018).
  10. The Two Isoforms of Lyn Display Different Intramolecular Fuzzy Complexes with the SH3 Domain, J. M. C. Teixeira, H. Fuentes, S. Bielskutė, M. Gairi, S. Żerko, M. Górka, W. Koźmiński, M. Pons,  Molecules, 23, 2731, (2018).
  11. Structure and dynamics of Helicobacter pylori nickel-chaperone HypA: an integrated approach using NMR spectroscopy, functional assays and computational tools, C. A. E. M. Spronk, S. Żerko, M. Górka, W. Koźmiński, B. Bardiaux, B. Zambelli, F. Musiani, M. Piccioli, P. Basak, F. C. Blum, R. C. Johnson, H. Hu, D. S. Merrell, M. Maroney, S. Ciurli J. Biol. Inorg. Chem., 23, 1309–1330, (2018).
  12. Conformational Equilibrium of Cinchonidine in C6D12 Solution. Alternative NMR/DFT Approach, S. Molchanov, T. Rowicki, A. Gryff-Keller, W. Koźmiński, J. Phys. Chem. A., 122, 7832-7841, (2018).
  13. Insight into human insulin aggregation revisited using NMR derived translational diffusion parameters, J. Sitkowski, W. Bocian, E. Bednarek, M. Urbańczyk, W. Koźmiński, P. Borowicz, G. Płucienniczak, N. Łukasiewicz, I. Sokołowska, L. Kozerski , J. Biomol. NMR , 71, 101-114, (2018).
  14. The RxLR Motif of the Host Targeting Effector AVR3a of Phytophthora infestans Is Cleaved Before Secretion, S. Wawra, F. Trusch, A. Matena, K. Apostolakis, U. Linne, I. Zhukov, J. Stanek, W. Koźmiński, I. Davidson, C. J. Secombes, Plant Cell , 29, 1184-1195, (2017).
  15. Joint non-uniform sampling of all incremented time delays for quicker acquisition in protein relaxation studies, M. Urbańczyk, M. Nowakowski, W. Koźmiński, K. Kazimierczuk, J. Biomol. NMR , 68, 155-161, (2017).
  16. 1H, 15N, 13C resonance assignment of plant dehydrin early response to dehydration 10 (ERD10), C. Cedeño, S. Żerko, P. Tompa, W. Koźmiński, Biomol. NMR Assign. , 11, 127–131 (2017).
  17. Reconstruction of non-uniformly sampled five-dimensional NMR spectra by signal separation algorithm, K. Kosiński, J. Stanek, M. J. Górka, S. Żerko, W. Koźmiński, J. Biomol. NMR, 68, 129-138, ( 2017).
  18. Structure and Dynamics of the Huntingtin Exon-1 N-Terminus: A Solution NMR Perspective, M. Baias, P. E. S. Smith, K. Shen, L. A. Joachimiak, S. Żerko, W. Koźmiński, J. Frydman, L. Frydman, J. Am. Chem. Soc., 139 1168-1176 , (2017).
  19. Metal-coupled folding as the driving force for the extreme stability of Rad50 zinc hook dimer assembly, T. Kochańczyk, M. Nowakowski, D. Wojewska, A. Ejchart, W. Koźmiński, A. Krężel,Sci. Rep., 6, 36346 , (2016).
  20. Five and four dimensional experiments for robust backbone resonance assignment of large intrinsically disordered proteins: application to Tau3x protein, S. Żerko, P. Byrski, P. Włodarczyk-Pruszyński, M. Górka, K. Ledolter, E. Masliah, R. Konrat, W. Koźmiński W. Koźmiński, J. Biomol. NMR, 65 , 193–203, (2016).
  21. Amino acid recognition for automatic resonance assignment of intrinsically disordered proteins, A. Piai, L. Gonnelli, I. C. Felli, R. Pierattelli, K. Kazimierczuk, K. Grudziąż, W. Koźmiński, A. Zawadzka-Kazimierczuk, W. Koźmiński, J. Biomol. NMR, 64 , 239–253, (2016) .
  22. Artifacts in time-resolved NUS: A case study of NOE build-up curves from 2D NOESY, R. Dass, P. Kasprzak, W. Koźmiński, K. Kazimierczuk,J. Magn. Reson. , 264, 108–116 (2016).
  23. 1H, 15N, 13C resonance assignment of human GAP43, A. G. Flamm, S. Żerko, A. Zawadzka-Kazimierczuk, W. Koźmiński, R. Konrat, N. Coudevylle Biomol. NMR Assign. , 10, 171–174 (2016). 
  24. Biochemical and structural characterization of the interaction between the Siderocalin NGAL/LCN2 and the N-terminal domain of its endocytic receptor SLC22A17, A. Cabedo Martinez, K. Weinhaupl, W. Lee, N. A. Wolff, B. Storch, S. Żerko, R. Konrat, W. Koźmiński, K. Breuker, F. Thévenod, N. Coudevylle, J. Biol. Chem. 291, 2917-2930, (2016).
  25. Nuclear overhauser spectroscopy of chiral CHD methylene groups, R. Augustyniak, J. Stanek, H. Colaux, G. Bodenhausen, W. Koźmiński, T. Hermann, F. Ferrage, W. Koźmiński, J. Biomol. NMR , 64, 27-37, (2016).
  26. Synthesis of rigid tryptophan mimetics by the diastereoselective Pictet–Spengler reaction of β3-homo-tryptophan derivatives with chiral α-amino aldehydes, M. Slupska, K. Pulka-Ziach, E. Deluga, P. Sosnowski, B. Wilenska, W. Koźmiński, A. Misicka J. Pept. Sci. , 21, 893-904, (2015).
  27. High resolution 4D HPCH experiment for sequential assignment of 13C-labeled RNAs via phosphodiester backbone, S. Saxena, J. Stanek, M. Cevec, J. Plavec W. Koźmiński, J. Biomol. NMR 63, 291-298, (2015).
  28. Six- and seven-dimensional experiments by combination of sparse random sampling and projection spectroscopy dedicated for backbone resonance assignment of intrinsically disordered proteins, S. Żerko, W. Koźmiński, J. Biomol. NMR 63,  83-290, (20 15) .
  29. 13C-detected NMR experiments for automatic resonance assignment of IDPs and multiple-fixing SMFT processing, P. Dziekański, K. Grudziąż, W. Koźmiński, A. Zawadzka-Kazimierczuk J. Biomol. NMR , 62, 179-190, (2015) .
  30. The solution structure of the MANEC-type domain from Hepatocyte Growth Factor Activator Inhibitor 1 reveals an unexpected PAN/apple domain-type fold. Z. Hong, M. Nowakowski, C. Spronk, S. V. Petersen, P. A. Andreasen, W. Koźmiński, F. A. A. Mulder, J. K. Jensen Biochem. J. 466 (2) 299-309, (2015) .
  31. 1H, 15N, 13C resonance assignment of human osteopontin, G. Platzer, S. Żerko, S. Saxena, W. Koźmiński, R. Konrat, Biomol. NMR Assign. 9 (2) , 289-292, (2015) .
  32. "CON-CON" assignment strategy for highly flexible intrinsically disordered proteins, A. Piai, T. Hošek, L. Gonnelli, A. Zawadzka-Kazimierczuk, W. Koźmiński, B. Brutscher, W. Bermel, R. Pierattelli, I. C. Felli J. Biomol. NMR, 60, 209-218, (2014).
  33. Analysis of Complex Reacting Mixtures by Time-Resolved 2D NMR, R. Dass, W. Koźmiński, K. Kazimierczuk Anal. Chem. 87 (2), 1337–1343, (2015) .
  34. Comparison of electrochemical- and nuclear magnetic resonance spectroscopy methods for determination of diffusion coefficients in gel environment, B. Adrjan, M. Karbarz, W. Koźmiński, Z. Stojek Electrochim. Acta. 144, 228-234, (2014).
  35. C4′/H4′ selective, non-uniformly sampled 4D HC(P)CH experiment for sequential assignments of 13C-labeled RNAs, S. Saxena, J. Stanek, M. Cevec, J. Plavec, W. Koźmiński J. Biomol. NMR 60, 91-98, (2014).
  36. Accelerating Diffusion-Ordered NMR Spectroscopy by Joint Sparse Sampling of Diffusion and Time Dimensions, M.Urbańczyk, W. Koźmiński, K. Kazimierczuk, Angew. Chem. Int. Ed. 53 (25), 6464-6467, (2014).
  37. NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme, M. Jaremko, Ł. Jaremko, M. Nowakowski, M. Wojciechowski, R. H. Szczepanowski, R. Panecka, I. Zhukov, M. Bochtlerd, A. Ejchart, J. Struct. Biol. 185 (1), 69-78, (2014).
  38. High-dimensionality 13C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins, W. Bermel, I. C. Felli, L. Gonelli, W. Koźmiński, A. Piai, R. Pierattelli, A. Zawadzka-Kazimierczuk, J. Biomol. NMR, 57, 353-361, (2013).
  39. A method for joint sparse sampling of time and gradient domains in diffusion-ordered NMR spectroscopy, M. Urbańczyk, K. Kazimierczuk, Signal Processing Symposium (SPS), 2013. IEEE (2013).
  40. 4D Non-uniformly sampled C,C-NOESY experiment for sequential assignment of 13C,13N-labeled RNAs, J. Stanek, P. Podbevšek, W. Koźmiński, J. Plavec, M. Cevec,J. Biomol. NMR 57, 1-9 (2013).
  41. Complex formation of fenchone with α-cyclodextrin: NMR titrations, M. Nowakowski, A. Ejchart, Journal of Inclusion Phenomena and Macrocyclic Chemistry , DOI:10.1007/s10847-013-0356-4
  42. Protonation-dependent conformational variability of intrinsically disordered proteins, L. Geist, M. A. Henen, S. Haiderer, T. C. Schwarz, D. Kurzbach, A. Zawadzka-Kazimierczuk, S. Saxena, S. Żerko, W. Koźmiński, D. Hinderberger, R. Konrat, Protein Science, 22 (9), 1196-1205 (2013).
  43. Peptides and peptidoaldehydes as substrates for the Pictet–Spengler reaction, K. Pułka, M. Słupska, A. Puszko, M. Misiak, M. Wilczek, W. Koźmiński, A. Misicka, J. Pep. Sci. 19 (7), 433-440 (2013).
  44. Selective diagonal-free 13C,13C-edited aliphatic–aromatic NOESY experiment with non-uniform sampling, J. Stanek, M. Nowakowski, S. Saxena, K. Ruszczyńska-Bartnik, A. Ejchart, W. Koźmiński, J. Biomol. NMR, 56, 217-226, (2013).
  45. Sialorphin and its analog as ligands for copper(II) ions, E. Kamysz, A. Kotynia, Ż. Czyżnikowska, M. Jaremko, Ł. Jaremko, M. Nowakowski, J. Brasun, Polyhedron, 55,  216–224, (2013).
  46. Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation, J. Stanek, S. Saxena, L. Geist, R. Konrat, W. Koźmiński, Angew. Chem. Int. Ed. 52 (17), 4604-4606 (2013).
  47. Biosynthetic engineered B28K–B29P human insulin monomer structure in water and in water/acetonitrile solutions, P. Borowicz, W. Bocian, J. Sitkowski, E. Bednarek, D. Mikiewicz-Syguła, D. Kurzynoga, D. Stadnik, W. Surmacz-Chwedoruk, W. Koźmiński, L. Kozerski J. Biomol. NMR, 55, 303-309, (2013).
  48. Impact of Calcium Binding and Thionylation of S100A1 Protein on Its Nuclear Magnetic Resonance-Derived Structure and Backbone Dynamics, M. Nowakowski, K. Ruszczyńska-Bartnik, M. Budzińska, Ł. Jaremko, M. Jaremko, K. Zdanowski, A. Bierzyński, A. Ejchart, Biochemistry, 52 (7), 1149–1159 (2013).
  49. Iterative Thresholding Algorithm for Multiexponential Decay Applied to PGSE NMR Data M. Urbańczyk, D. Bernin, W. Koźmiński, and K. Kazimierczuk,  Anal. Chem. 85 (3), 1828-1833 (2013).
  50. Study of near-symmetric cyclodextrins by compressed sensing 2D NMR M. Misiak, W. Koźmiński, K. Chmurski, K. Kazimierczuk, Magn. Res. Chem., 51, 101-115 (2013).
  51. Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain Z. Orbán-Németh, M. A. Henen, L. Geist, S. Żerko, S. Saxena, J. Stanek, W. Koźmiński, W., F. Propst, R. Konrat, Biomol. NMR Assign. 8 (1), 123-127, (2014).
  52. 1H, 13C and 15N resonance assignments of human BASP1 L. Geist, A. Zawadzka-Kazimierczuk, S. Saxena, S. Żerko, W. Koźmiński, R. Konrat, Biomol. NMR Assign. 7 (2), 315-319, (2013).
  53. A comparison of convex and non-convex compressed sensing applied to multidimensional NMR , K. Kazimierczuk, V. Y. Orekhov, J. Magn. Reson., 223, 1-10 (2012).
  54. 1H, 13C, and 15N backbone and side chain resonance assignments of the C-terminal DNA binding and dimerization domain of v-Myc G. Kizilsavaş, S. Saxena, S. Żerko, W. Koźmiński, K. Bister, R. Konrat, Biomol. NMR Assign. 7 (2), 321-324, (2013).
  55. Is there any proton exchange between ammoniumions localized within the d(G3T4G4) 2 quadruplex? P. Šket, W. Koźmiński, J. Plavec, Acta Chim. Slov. 59, 473-477 (2012).
  56. TSAR: A program for automatic resonance assignment using 2D cross-sections of high dimensionality, high-resolution spectra A. Zawadzka-Kazimierczuk, W. Koźmiński, M. Billeter J. Biomol. NMR, 54, 81-95, (2012).
  57. Speeding up sequence specific assignment of IDPs W. Bermel, I. Bertini, I. C. Felli, L. Gonnelli, W. Koźmiński, A. Piai, R. Pierattelli, J. Stanek J. Biomol. NMR, 53, 293-301, (2012).
  58. Insights from impedance spectroscopy into the mechanism of thermal decomposition of  M(NH2BH3), M = H, Li, Na, Li0.5Na0.5, hydrogen stores K. J. Fijalkowski, R. Jurczakowski,  W. Koźmiński W. Grochala Phys. Chem. Chem. Phys., 14, 5778-5784 (2012).
  59. High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins A. Zawadzka-Kazimierczuk, W. Koźmiński, H. Šanderová, L. Krásný J. Biomol. NMR, 52, 329-337, (2012).
  60. 1H, 13C, and 15N chemical shifts assignments for human endothelial monocyte-activating polypeptide EMAP II D. Lozhko,J. Stanek, K. Kazimierczuk., A. Zawadzka-Kazimierczuk, W.Koźminski, I. Zhukov, A. Kornelyuk Biomol. NMR Assign. 7, 25-29, (2013).
  61. Crystal and electronic structure, lattice dynamics and thermal properties of Ag(i)(SO3)R (R = F, CF3) Lewis acids in the solid state W. Grochala, M. K. Cyrański, M. Derzsi, T. Michałowski, P. J. Malinowski Z. Mazej, D. Kurzydłowski, W. Koźmiński, A. Budzianowski P. J. LeszczyńskDalton Trans., 41, 2034-2047 (2012).
  62. Suppression of sampling artefacts in high-resolution four-dimensional NMR spectra using Signal Separation Algorithm. J. Stanek, R. Augustyniak, W. Koźmiński, J. Magn. Reson., 214, 91-102 (2012).
  63. Accelerated NMR Spectroscopy by Using Compressed Sensing. K. Kazimierczuk, VY. Orekhov, Angew. Chem. Int. Ed. 50 5556-5559 (2011).
  64. Polymorphism of a model arylboronic azaester: Combined experimental and computational studies. K. Durka, A. Hoser, R. Kamiński, S. Luliński, J. Serwatowski, W. Koźmiński, K. Woźniak, Cryst. Growth Des., 11, 1835–1845 (2011).
  65. Phase transition induced improvement in H2 desorption kinetics: the case of the high-temperature form of Y(BH4)3. T. Jaroń, W. Koźmiński, W. Grochala, Phys. Chem. Chem. Phys., 13, 8847–8851 (2011).
  66. 5D 13C detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion. J. Nováček, A. Zawadzka-Kazimierczuk, V. Papoušková, L. Žídek, H. Šanderová, L. Krásný, W. Koźmiński, V. Sklenář, J. Biomol. NMR, 50, 1-11 (2011).
  67. Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution-enhanced 5D experiments, V. Motáčková, J. Nováček, A. Zawadzka-Kazimierczuk, K. Kazimierczuk, L. Žídek, H. Šanderová, L. Krásný, W. Koźmiński, V. Sklenář, J. Biomol. NMR, 48, 169-177 (2010).
  68. Non-uniform frequency domain for optimal exploitation of non-uniform sampling. K. Kazimierczuk, A. Zawadzka-Kazimierczuk, W. Koźmiński, J. Magn. Reson., 205, 286–292 (2010).
  69. Polymorphism of Fluoroargentates(II): Facile collapse of a layered network of α-K2AgF4 due to the insufficient size of the potassium cation. D. Kurzydłowski, M. Derzsi, A. Budzianowski, Z. Jagličić, W. Koźmiński, Z. Mazej, W. Grochala, Eur. J. Inorg. Chem., 2919–2925 (2010).
  70. Iterative algorithm of Discrete Fourier Transform for processing randomly sampled NMR data sets. J. Stanek, W. Koźmiński, J. Biomol. NMR, 47, 65-77 (2010).
  71. A Traceless, Solid-Supported Synthesis of b-Turn Mimetics Based on the Hexahydropyrazino [1,2-a]pyrazine-1,2-dione Scaffold. A. Mieczkowski, W. Koźmiński, J. Jurczak, Synthesis, 2, 221–232 (2010).
  72. A set of 4D NMR experiments of enhanced resolution for easy resonance assignment in proteins, A. Zawadzka-Kazimierczuk, K. Kazimierczuk, W. Koźmiński, J. Magn. Reson., 202, 109-116 (2010).
  73. Complete 1H and 13C signal assignment of prenol-10 with 3D NMR spectroscopy. M. Misiak, W. Koźmiński, M. Kwasiborska, J. Wójcik, E. Ciepichal, E. Swiezewska, Magn. Res. Chem., 47, 825–829 (2009).
  74. KAgF3, K2AgF4 and K3Ag2F7: Important Steps Towards a Layered Antiferromagnetic Fluoroargentate (II). Z. Mazej, E.  Goreshnik, Z. Jaglicic, B. Gawel, W. Lasocha, D. Grzybowska, T. Jaron, D. Kurzydłowski, P. Malinowski, W. Koźmiński, J. Szydlowska, P. Leszczynski, W. Grochala, CrystEngComm., 11, 1702-1710 (2009).
  75. Spatial structure and NMR spectra of strained [2.2.2]cyclophanes. H. Dodziuk, M. Ostrowski, K. Ruud, J. Jaźwiński, H. Hopf, W. Koźmiński, Magn. Res. Chem., 47, 407-414 (2009).
  76. Narrow peaks and high dimensionalities: exploiting the advantages of random sampling. K. Kazimierczuk, A. Zawadzka, W. Koźmiński, J. Magn. Reson., 197, 219-228 (2009).
  77. Determination of heteronuclear coupling constants from 3D HSQC-TOCSY experiment with optimized random sampling of evolution time space. M. Misiak, W. Koźmiński, Magn. Res. Chem., 47, 205-209 (2009).
  78. Determination of spin-spin couplings from ultra high resolution 3D NMR spectra obtained by optimized random sampling and Multidimensional Fourier Transformation. K. Kazimierczuk, A. Zawadzka, W. Koźmiński, I. Zhukov, J. Am. Chem. Soc., 130, 5404-5405 (2008).
  79. Optimization of random time domain sampling in multidimensional NMR. K. Kazimierczuk, A. Zawadzka, W. Koźmiński, J. Magn. Reson. 192, 123-130 (2008).
  80. Direct insight into insulin aggregation by 2D NMR complemented by PFGSE NMR. W. Bocian, J. Sitkowski, A. Tarnowska,  E. Bednarek, R. Kawęcki, W. Koźmiński, L. Kozerski, Proteins, 71, 1057-1065 (2008).
  81. Diastereoselective Pictet-Spengler condensation of tryptophan with a-amino aldehydes as chiral carbonyl components. K. Pułka, P. Kulis, D. Tymecka, Ł. Frankiewicz, M. Wilczek, W. Koźmiński, A. Misicka, Tetrahedron, 64, 1506-1514 (2008).
  82. (F,H), J(C,H) and J(H,H) couplings involving the individual methyl group protons in 1,2,3,4-tetrachloro-5,6,7,8-tetrafluoro-9-methyltriptycene. Evidence of blue-shifting hydrogen Bond, I. Czerski, K. Kamieńska-Trela, W. Koźmiński, T. Ratajczyk, S Szymański, J. Wójcik, Magn. Res Chem., 45, 1040-1044 (2007).
  83. Lineshapes and Artifacts in Multidimensional Fourier Transform of Arbitrary Sampled NMR Data Sets, K. Kazimierczuk, A. Zawadzka, W. Koźmiński, I. Zhukov, J. Magn. Reson., 188, 344-356 (2007).
  84. Three-dimensional NMR Spectroscopy of organic molecules by random sampling of evolution time space and multidimensional Fourier transform. M. Misiak, W. Koźmiński, Magn. Res Chem., 45, 171-174 (2007).
  85. Random sampling of evolution time space and Fourier transform processing. K. Kazimierczuk, A. Zawadzka, W. Koźmiński, I. Zhukov, J. Biomol. NMR, 36, 157-168 (2006).
  86. On the Influence of Low-Frequency Magnetic Field Disturbances on Basic High Resolution NMR Experiments K. Kazimierczuk, W. Koźmiński, Pol. J. Chem., 80, 1119-1124 (2006).
  87. The studies of tautomerism in 6-mercaptopurine derivatives by 1H–13C, 1H–15N NMR and 13C, 15N CPMAS-experimental and quantum chemical approach. L. Pazderski, I. Łakomska, A. Wojtczak, E. Szłyk, J.  Sitkowski, L. Kozerski, B. Kamieński, W. Koźmiński, J. Tousek, R.  Marek, J. Mol. Struct., 785, 205-215 (2006).
  88. Two-dimensional Fourier transform of arbitrarily sampled NMR data sets. K. Kazimierczuk, W. Koźmiński, I. Zhukov, J. Magn. Reson. 179, 323-328 (2006).
  89. Efficient compensation of low-frequency magnetic field disturbances in NMR with fluxgate sensors. K. Kazimierczuk, W. Koźmiński, J. Magn. Reson. 174, 287-291 (2005).
  90. A protein backbone y and f angle dependence of 2JN(i),Cα(i-1): the new NMR experiment and quantum chemical calculations. W. Koźmiński, I. Zhukov, M. Pecul, J. Sadlej, J. Biomol. NMR, 31, 87- 95, (2005).


  1. High-dimensional NMR methods for intrinsically disordered proteins studies, K. Grudziąż, A. Zawadzka-Kazimierczuk, W. Koźmiński, Methods , 148, 81-87, (2018).
  2. Applications of high dimensionality experiments to biomolecular NMR M. Nowakowski, S. Saxena, J. Stanek, S. Żerko, W. Koźmiński, Prog. Nucl. Magn. Reson. Sp. 90-91, 49-73 (2015).
  3. High-Dimensional NMR Spectra for Structural Studies of Biomolecules, K. Kazimierczuk, J. Stanek, A. Zawadzka-Kazimierczuk, W. Koźmiński, ChemPhysChem, 14, 3015-3025 (2013).
  4. Sparse sampling. W. Koźmiński in G.C.K. Roberts (ed.), Encyclopedia of Biophysics, Springer-Verlag Berlin Heidelberg 2012
  5. Generalized Fourier transform for non-uniform sampled data. K. Kazimierczuk, M, Misiak, J. Stanek, A. Zawadzka-Kazimierczuk, W. Koźmiński, Topics in Current Chemistry, 316, 79-124 (2012).
  6. Random sampling in multidimensional NMR spectroscopy. K. Kazimierczuk, J. Stanek, A. Zawadzka-Kazimierczuk, W. Koźmiński, Prog. Nucl. Mag. Res. Sp., 57,420–434 (2010).
  7. Progress in structural studies of proteins by NMR spectroscopy. K. Kazimierczuk, M. Misiak, A. Zawadzka, W. Koźmiński, Polimery, 52, 736-744 (2007).
  8. NMR of cyclodextrins and their complexes, A. Ejchart, W. Koźmiński, in Cyclodextrins and their complexes. pp. 231-254, Ed. H. Dodziuk, Wiley-VCH GmbH & Co. KGaA, Weinheim 2006.
  9. Podstawowe techniki eksperymentalne spektroskopii NMR w fazie ciekłej. W. Koźmiński, Wiadomości Chemiczne, 59, 107-120, (2005).
  10. NMR Studies of Chiral Recognition by Cyclodextrins. H. Dodziuk, W. Koźmiński, A. Ejchart, Chirality, 16, 90-105 (2004).
  1. Structure and dynamics of Helicobacter pylori nickel-chaperone HypA: an integrated approach using NMR spectroscopy, functional assays and computational tools, C. A. E. M. Spronk, S. Żerko, M. Górka, W. Koźmiński, B. Bardiaux, B. Zambelli, F. Musiani, M. Piccioli, P. Basak, F. C. Blum, R. C. Johnson, H. Hu, D. S. Merrell, M. Maroney, S. Ciurli J. Biol. Inorg. Chem., In Press,  (2018).


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