Spectrometer Status

CFI 600

ORDCF 600

Related Facilities

• Biomolecular Interactions & Conformations Facility
• Biological Mass Spectrometry Laboratory
• Functional Proteomics Facility
• Macromolecular Crystallography Facility
• MALDI Mass Spectrometry Facility
• Peptide Synthesis Facility

NMR Facility Overview

The Biomolecular NMR Facility at Western University houses three high field NMR instruments, two Varian INOVA 600 MHz and one UNITY 500 MHz spectrometers, and a variety of accessories that allow a large number of biological NMR experiments to be done.

The facility has supported research projects that focus on calcium signaling, protein folding, enzyme catalysis, signal transduction, membrane structure and function, bone mineralization and "jumping genes".

Capabilities of the facility include:
• Characterization of small biological molecules
• Three-dimensional structure determination of soluble proteins in solution
• Drug and receptor interactions
• Protein dynamics
• Mapping of protein-protein binding interfaces
• Determine changes in protein conformation

Funding Organizations:

 

About NMR

Nuclear Magnetic Resonance (NMR) Spectroscopy is a non-destructive method that allows the structural and dynamic characterization of molecules in solution. Developed by Purcell and Bloch in 1945 (Nobel Prize in Physics 1952) it relies on the absorption of radiofrequency energy by nuclei within a strong magnetic field. Since nuclei within a given molecule have different bonding arrangements or neighbouring atoms, each nucleus gives rise to a characteristic resonant frequency. In biomolecular NMR, the identification of individual proteins and nucleic acids uses molecules enriched with 13C and 15N to allow assignment of individual nuclear frequencies using multi-dimensional techniques (Ernst, Nobel Prize in Chemistry 1991). This information can be used to determine the three-dimensional structures of peptides and proteins in solution (Wuthrich, Nobel Prize in Chemistry 2002), their regions and surfaces of interaction with drugs and other molecules, binding affinities and conformational dynamics over a wide timescale (psec-sec). NMR methods also form the foundation for medical diagnostics such as magnetic resonance imaging (MRI) (Lauterbur, Mansfield, Nobel Prize in Medicine & Physiology, 2003)