A molecular level knowledge of structure and dynamics is critical for understanding biochemical reaction mechanisms and molecular recognition processes. Such an understanding supports biotechnology and bioengineering efforts in areas ranging from pharmaceutical development to biomaterials design. Several research programs, involving nuclear magnetic resonance (NMR) spectroscopy, are under way at IBBR in which scientists are developing and utilizing state-of-the art measurement methods, models and databases to study biomolecular structure, dynamics and interactions in solution. Research projects include investigations into the structure and dynamics of complex therapeutics, membrane proteins and receptors, and nucleic acids and nucleic acid-protein complexes. NMR measurements are also used to study protein folding, stability and reaction kinetics.

A 900 MHz (21.14 Tesla) NMR spectrometer equipped with a Cryoprobe was installed in 2011 and became operational in early 2012. This ultra-high field NMR spectrometer offers increase sensitivity and resolution and provides opportunities for developing new NMR applications that take advantage of unique physical properties of biomolecules at ultra-high magnetic fields.