This is the only research group in Poland that deals with the methodology of NMR spectroscopy in the liquid phase. The main field of study of this group is exploring new, effective methods of NMR spectroscopy and their application in structural research in chemistry and biochemistry. The most important of those are methods that avoid limitations associated with sampling procedures and signal processing, which are one of the most significant challenges in modern NMR spectroscopy.


Professor Wiktor Koźmiński



Professor Wiktor Koźmiński,,
UW BCRC,phone: 48 22 55 26519,
room number 007

Karolina Madrak Ph.D.,
Michał Nowakowski Ph.D.,
Saurabh Saxena M.Sc.,
Jan Stanek M.Sc.,
Mateusz Urbańczyk M.Sc.,
Anna Zawadzka – Kazimierczuk Ph.D.,
Szymon Żerko M.Sc.


This group’s research activities in the field of measuring multidimensional NMR spectra focus on: recording highly dimensional spectra, new methods of signal assignment to proper atoms in biopolymers, effective identification of structural bonds, application of new methods in research on fully or partially unstructured proteins, development of a method for artifact removal from spectra, which allows scientists for full analysis of spectra characterized by highly changeable signal amplitudes, application of Compress Sensing method for processing of NMR spectra. Moreover, this group is interested in the development of measuring the diffusion coefficient and new NMR spectroscopy methods for precise and thorough measurements of scalar and residual dipolar spin-spin coupling from 3-4D spectra.

Instruments used by the group

NMR 600 MHz DDR2 Spectrometer from Agilent:

  • “one-NMR” probe, two channels 1H/19F and broadband 15N-31P (+2H channel), z-gradient;
  • HCN probe, three channels 1h/13C/15N (+2H channel), xyz-gradients;
  • “Penta” probe, four channels 1H/13C/15N/31P (+2H channel), z-gradient;
  • 12 position autosampler

NMR 800 MHz DDR2 spectrometer from Agilent:

  • Two parallel receiver channels
  • Probe HCN, three channels 1H/13C/15N (+2H channel), z-gradients
  • Cryogenic probe, three channels 1H/13C/15N (+2H channel),  z-gradients, built-in preamplifiers 1H & 13C
  • Probe “Bio-MAS” for powder samples, three channels 1H/13C/15N, rotor size 3.2mm. MAS to 25kHz, inductor minimizing dielectric losses

Research services

Application of 600 MHz: NMR spectroscopy of proteins and nucleic acids in solutions, high-complexity organic samples:

  • 1 and 2 dimensional routine measurements COSY, TOCSY, NOESY, ROESY, HSQC, HMBC and others for small and medium organic particles
  • Measurements of DOSY diffusion and diffusion-partition coefficients
  • Experiments with random sparing sampling of 2D spectra for maximum possible resolution in frequency domain
  • Routine 3D measurement techniques for assignment of resonance peaks in proteins i.a. HNCO, HNCA HN(CO)CA, HNCACB, CBCA(CO)NH etc.
  • Routine 3D heteronuclear-partition techniques for NOE effect
  • Routine 2D and 3D techniques for nucleic acids
  • Experiments with random sparing sampling in 3-5D spectra, for assignment of peaks and measurements of structural bonds of proteins and nucleic acids
  • Research on fully or partially unstructured proteins
  • Experiments matching particular scientific problems

Application of 800 MHz: NMR spectroscopy of proteins and nucleic acids in solutions and solid phase:

  • All range of 600 MHz measurements and also:
  • Cases in which high sensitivity is needed – application of cryogenic probe, including samples with high concentration of salt
  • TROSY effect
  • Parallel detection (e.g. 1H and 13C)
  • 13C detection in fully or partially unstructured proteins and/or paramagnetic proteins
  • Research on proteins in solid phase