Protein NMR Projects

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY - FROM NUCLEAR INTERACTIONS TO MOLECULAR STRUCTURE

Our group is interested in the development of solid-state NMR methods for the characterization of molecular structure, dynamics and interactions at atomic resolution. Amongst systems of principal interest are membrane proteins or membrane-associated complexes. They constitute about 30% of a genome, and their structure determination is one of the most challenging problems in structural biophysics. Our group is well equipped with an array of NMR spectrometers available at the University of Guelph NMR Centre, including the only one in Canada 600 MHz/395 GHz Dynamic Nuclear Polarization NMR spectrometer.

Our interdisciplinary research spans a wide range of areas from quantum mechanics of spin interactions and developing new experimental ways to manipulate these interactions, to computational methods to molecular biology, biochemistry and biophysics. Below are just a few representative examples of the current projects.

  • Designing new experiments to determine protein structure. A typical NMR experiment consists of a sequence of radio-frequency pulses, which can be designed to rotate spins, and to manipulate spin Hamiltonians, e.g., cancel or amplify interactions, or to tailor them to a specific, optimal form. We are always interested in developing new methods for specific experimental needs.
  • Interpretation of nuclear spin relaxation experiments. In an NMR experiment, nuclear spins are perturbed from equilibrium by radio-frequency pulses. If let evolve on their own, they will eventually come back to equilibrium at a rate that depends on the molecular motions, which occur on a wide range of scales (e.g., the entire molecule can slowly diffuse, specific domains can experience intermediate motions on a microsecond time scale, and atoms can undergo local diffusive motions on a subnanosecond time scale). From the analysis of nuclear relaxation rates one can derive both the site-specific time scales and amplitudes of motions. This information is directly related to how molecules function.
  • We apply these methods to problems of medical/biotechnological relevance, e.g., design of new pharmacological drugs, understanding of the molecular origins of diseases, design of novel biomaterials.

For the most up-to-date information on the current research see our publications

We are seeking MSc and PhD students to work in our group

If interested, do not hesitate to email Vlad Ladizhansky directly, and inquire about current possibilities: vladizha@uoguelph.ca.