Nuclear Magnetic Resonance (NMR) spectroscopy is one of the principal techniques used to obtain physical, chemical, electronic and structural information about molecules. It is a powerful technique that can provide atomic resolution information on the topology, dynamics and three-dimensional structure of molecules in solution and the solid state. The breadth and quality of information attainable from NMR measurements makes it unique among spectroscopic tools.

Example applications include:

  • Structure determination; either at atomic resolution for highly-ordered macromolecules, or through defining structural propensities of more dynamic molecules such as unfolded proteins or carbohydrates.
  • NMR can provide in-depth characterisation of intermolecular interactions, making it a powerful tool in drug discovery.
  • Dynamics measurements on large molecules (macromolecules), to determine how such processes control biological function, for example in the folding of proteins, intermolecular signalling and biological catalysis.

Introduction of specific labels allows the probing of particular regions of interest in proteins, for example using fluorine compounds to probe the environment in active sites of enzymes, or the dynamics of peptides in complex with larger proteins, which have been perdeuterated to render them NMR silent.


Dr Matthew Cliff | matthew.cliff@manchester.ac.uk | Tel: +44 (0)161 306 5179


In March 2012 the MIB took delivery of a new 800 MHz Bruker NMR spectrometer, along with upgrades to existing 600 and 500 MHz spectrometers. These instruments have allowed measurement of:

  • extremely high resolution spectra of carbohydrate molecules
  • ps-ns dynamic measurements on enzyme complexes
  • structure determination of an fnIII domain in the context of a fibronectin fragment
  • measurement of anti-aggregation effects of excipient in antibody solutions

We have close links with Bruker who have contributed four 4-year fully funded industrial PhD studentships.


We advise on the type of NMR experiments that will be most suitable, appropriate and informative for a particular project, and provide help with setting up experiments and training for regular NMR users. Protein sample check and full chemistry data set service is available on request. Experienced academic and commercial users are also welcome.


MIB has both state-of-the-art very high magnetic field strength instruments, and more economical lower field instruments. All are designed for solution measurements.

  • 800 MHz Bruker four-channel liquid-state spectrometer
    Equipped with a high sensitivity TCI cryoprobe with cooled proton and carbon channel.
  • 600 MHz Bruker four-channel liquid-state spectrometer
    Equipped with a high sensitivity TXI cryoprobe with cooled proton channel.
  • 500 MHz Bruker five-channel liquid-state spectrometer
    Equipped with a high sensitivity QXI cryoprobe with cooled proton, fluorine and carbon channel. Fluorine NMR provides additional information to the standard nuclei set of 1H, 13C and 15N.
  • 400 MHz NMR spectrometer
    Carbon and proton detection for small molecule work. This is a walk-up service spectrometer for determining the results of chemical syntheses.

Equipment sharing

The facility is a lead member of the resoN8 equipment sharing initiative, which encourages equipment sharing between NMR facilities across the North of England. We have hosted users from Leeds, York, Sheffield and Hull and frequently use spectrometers in Sheffield through this initiative. We also share best practice through our wiki and through joint training activities, which includes and annual week long “NMR week” on NMR theory and practice. Please visit our wiki.