... understanding life in molecular detail

Dr Lars Kuhn

Nuclear Magnetic Resonance (NMR); real-time NMR; protein folding; hyperpolarization


We develop nuclear magnetic resonance (NMR) hyperpolarization and rapid mixing methods for acquiring NMR spectra of protein folding events at high spectral and temporal resolution ‘in situ’.

Current major projects include:
  • ’Real-time’ nD-NMR investigation of protein folding.
  • Development of NMR hyperpolarization methods.
  • Development of rapid mixing technology for ‘real-time’ NMR.
  • Improving NMR-assisted enantiodiscrimination methods.
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BioNMR Support Scienstist

M.Sc. Award “Chemistry” (University of Bonn); M.Sc. & Ph.D. Scholar of the German National Academic Foundation; EPSRC Departmental Training Award; MRC Award for Young Scientists; DFG Young Investigator Award; Member of the Cluster of Excellence “Centre for Molecular Physiology of the Brain”


Miall 4.21A
School of Molecular and Cellular Biology
0113 343 3024
l.kuhn@leeds.ac.uk

Selected Publications

  1. Pérez-Trujillo M, Parella T, Kuhn LT. NMR-aided differentiation of enantiomers: Signal enantioresolution. Anal Chim Acta. 2015; 876:63.

  2. Kuhn LT. Photo-CIDNP NMR spectroscopy of amino acids and proteins. Top Curr Chem. 2013; 338:229-300.

  3. Rogne P, Ozdowy P, Richter C, Saxena K, Schwalbe H, Kuhn LT. Atomic-level structure characterization of an ultrafast folding mini-protein denatured state. PLoS One. 2012; 7:e41301.

  4. Schmidt M, Sun H, Rogne P, Scriba GK, Griesinger C, Kuhn LT, Reinscheid UM. Determining the absolute configuration of (+)-mefloquine HCl, the side-effect-reducing enantiomer of the antimalaria drug Lariam. J Am Chem Soc. 2012; 134:3080.