EMSL’s high-resolution liquids nuclear magnetic resonance (NMR) instruments are used to characterize the three-dimensional structure, dynamics, and interactions of biological macromolecules.

Our sensitive, cryogenically cooled, triple-resonance (1H, 13C, 15N) probes enable characterization of stable-isotope labeled samples at low concentrations, where proteins are less prone to self-assembly and aggregate. The high sensitivity also allows characterization of samples extracted from natural sources, where isotope labeling is usually impossible. Several of the instruments also have a fourth channel for 2H decoupling that is required to study much larger proteins and complexes, or a channel for detecting 31P that is required to study proteins, nucleic acids, and metabolites containing this atom.    

Liquid state NMR can measure the distance between protons to determine the three-dimensional structure of proteins less than ~30 kDa.

Research application

Supporting the Structural Biology Integrated Research Platform, liquid state NMR can be used to investigate nucleic acids, peptides, and heterogeneous cell-wall biopolymers, such as lignin and oligosaccharides.

Available instruments

• 800 MHz Bruker Avance Neo (Tava), 24-position SampleCase sample changer, supporting 1H, 13C, 15N, 19F, and 31P nuclei across two CryoProbes. 
• 750 MHz Bruker Avance III (Bokan), with 510-position cooled SampleJet sample changer, with a 1H, 13C, 15N CryoProbe and a broadband X-nuclei probe. 
• 750 MHz Varian VNMRS (Rainier), with a 1H, 13C, 15N probe and a broadband X-nuclei probe.  
• 600 MHz Agilent DD2 (Baker): 5 mm HCN Z-gradient cold probe with VT control of 0 to 50 °C 
• 600 MHz Agilent VNMRS (Hood): 5 mm HCN salt tolerant Z-gradient cold probe with VT control of 0 to 80 °C 
• 700 MHz Bruker Avance Neo (Glacier): 5 mm HCN TCI CryoProbe with VT control of -10 to 60 °C

Tips for success

• To get useful NMR data of proteins and other biomacromolecules, it is essential to prepare a suitable sample of the system of interest.
• Users new to biomolecular NMR spectroscopy should consult with us to identify a sample system and optimal conditions for collection of the high-quality data. Collaboration and consultation with us throughout the duration of your project is a highly recommended “best practice” to ensure success.
• Proteins are prone to aggregation, degradation, and precipitation, but must remain intact and dissolved in solution conditions that minimize such behavior. In addition, proteins of interest typically must be labeled with NMR-active stable isotopes (¹³C, ¹⁵N, and sometimes ²H).