The National Deuteration Facility offers the facilities, staff and expertise to produce molecules where all or part of the molecular hydrogen is in the form of the stable (non-radioactive) isotope deuterium (2H).

This is of benefit as it enables scientists to use neutron scattering or Nuclear Magnetic Resonance (NMR) spectroscopy more effectively in the investigation of the relationship between the structure and function of proteins, DNA, synthetic polymers or other materials known as 'soft matter'. When molecules are placed in front of a neutron beam, hydrogen and deuterium scatter neutrons quite differently (ie they have a different scattering length density). Molecular deuteration of subunits of a molecule, or complex, enables the creation of contrast between these components and those containing 1H in a system that would otherwise offer far less information. Thus, it is possible to observe the arrangement of subunits of an enzyme, or changes in shape when molecules interact or become active/inactive, using molecular deuteration and small angle neutron scattering. This can be done with molecules in solution under relevant real life conditions using the small-angle neutron scattering instrument Quokka at the OPAL reactor.

Another application is to produce deuterated molecules for neutron crystallography where deuteration leads to a much reduced backgorund in the data and enables use of a smaller crystal. This technique may be used to obtain information about the position of key hydrogens in a molecule, for example in the region responsible for catalysis by an enzyme. Thus neutron crystallography of deuterated proteins may augment information obtained from X-ray crystal structures that have ambiguity in the position of hydrogens in the molecule (due to X-rays lesser ability to 'see' hydrogen).

A third application involves the use of neutron reflectivity (Platypus at the OPAL Reactor) and selective deuteration of lipid molecules in model biomembrane bilayer systems in order to obtain information about the behaviour of various components during events such as disruption by toxins or attack by enzymes, as well as the position and shape of membrane bound proteins.

More information on Molecular Deuteration (Biological and Chemical Deuteration Laboratories)
Contact: Professor Peter Holden
Phone: + 61 2 9717 3991
Email: ndf-enquiries@ansto.gov.au