Taylor, Natalie-Rose, Austerberry, James, Laity, Peter and Belton, Daniel J. (2012) The application of simultaneous electric and magnetic fields to aid protein crystallisation. In: Nanoformulation 2012, 27th May – 1st June 2012, Barcelona, Spain. (Unpublished)

Electric fields have a beneficial effect on protein crystallisation. This is because of amino acids contributing to an overall charge for the protein once they have bonded together via a peptide link. Taking this into consideration crystals are able to form when an electrical field is applied because of the potential gradient the current created which causes the migration of the protein through its media resulting in the build up of crystals. The downside to using only an electric field however is that different proteins have different resistances to a change in voltage, and that the alignment would only be along one field.
Magnetic fields, when applied to proteins induce diamagnetic behaviour. The peptide bond between each individual amino acid plays an important role in this because it has a carbon-oxygen double bond. A double bond has been shown to exhibit a diamagnetic anisotropy and so in turn so would the peptide bond. This diamagnetic behaviour is exhibited in secondary structure proteins.
With the application of simultaneous fields the idea is that one field provides alignment on one plane and the second field on another. From that the protein molecules would be aligned and suspended in the solution at equally spaced intervals in a uniform manor. To further promote this a high protein concentration was used to condense the protein molecules together. The purpose of this research is ultimately to provide insights into how best to solve the structures of different proteins, which would provide us with advances from the application of this multi-field technique.