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Lewandowski group focuses on development and applications of solid-state and solution NMR to study structure, dynamics and interactions of biological systems. Please use the links to access more information. Our group is a part of solid-state NMR grouping located in Millburn House at the University of Warwick and Chemical Biology Research Facility.

Research Areas

Solid-State NMR Methodology Development | Protein structure determination and molecular interactions | Structural biology and engineering of systems involved in natural products biosynthesis | Protein dynamics


Research Areas

MAS rotors versus maximum spinning frequency
Solid-State NMR Methodology Development

We develop solid-state NMR methods for studying structures and dynamics of proteins.


  • NMR relaxation and methodology at 60-111 kHz magic angle spinning (PCCP 2015).
  • Characterisation of structure and dynamics of large protein complexes (JACS 2014, Angew. Chem. 2015)
  • Solvent PREs for characterisation of protein-protein interfaces in large complexes (JACS 2017)
Protein structure determination and molecular interactions

We employ a combination of different structural biology and biophysical methods led by solid-state and solution-state NMR to investigate structure, dynamics and interactions of various biological systems. We work on systems that are natural targets for solid-state NMR, e.g. nanocrystalline proteins, protein complexes (e.g. protein-antibody complexes and complexes from polyketide synthases), fibrils and membrane proteins and systems that benefit from combined solution/solid state NMR approaches. We are also interested in characterization of molecular interactions, in particular protein interactions with other proteins, ligands and nucleic acids.

Main areas:

  • natural products biosynthesis (polyketide synthases) (Nat. Chem. Biol. 2018)
  • peptidoglycan biosynthesis
Protein dynamics

We apply a variety of methods centered around NMR to characterize protein motions at atomic resolution.


  • dynamics of GB1 in a >300 kDa complex with full length immunoglobulin (Angew. Chem. 2015)
  • protein "dynamic transitions" through the lens of variable temperature relaxation measurements in a crystalline protein (Science 2015)
  • peptide plane fluctuations from joint 15N and 13C' relaxation measurements (PhysChemChemPhys 2015)
Structural biology and engineering of systems involved in natural products biosynthesis

We employ NMR-led integrated structural biology approach to study mechanistic details of various PKS/NRPS biosythetic pathways.