Nuclear Magnetic Resonance

Nuclear Magnetic Resonance

1. What does it do?

   • Determines structures of biological macromolecules
   • Study time dependent phenomena
     • Reaction kinetics
     • Molecular recognition
     • Protein folding
   • Energy levels of atomic nuclei are split by a magnetic field
     • Transitions between energy levels can be induced by exciting the sample with radiation whose frequency is equivalent to the energy difference between the two levels

2. Limitations

   • Low sensitivity
   • High complexity

3. New developments in NMR

   • Progress in spectromer technology has increased sensitivity and resolution of NMR
   • Theoretical advances
     • Better understanding of information from NMR
   • Advances in biochemical methods
     • Simple and fast preparation of samples
   • Heteronuclei can be incorporated into protein

4. Why NMR?

   • Probe molecules are in their natural state
     • Structure
     • Function
     • Dynamics
     • Interactions with ligands, proteins and membranes
   • No crystal packing effects
   • No need to crystallise
   • NMR is expensive and uses large equipment but structural and functional information can be found out

5. Peptide bond

   • Repeating unit throughout the protein
   • Allows NMR to work