Structural studies of macromolecules using NMR spectroscopy or X-ray crystallography can contribute enormously to our understanding of many biological processes. These techniques can also be used to elucidate the interaction between macromolecules. The function of RTP is to stop DNA replication when the proteins involved in replication reach the end of the chromosome. This revealed that a 3-helices are involved in the binding interaction, and that the 'wings' of RTP may not be contributing to binding. In collaboration with Dr. Matthew Wilce in the Crystallography Centre, we will work towards solving the structure of the whole complex.
Many bioactive molecules have intracellular sites of action.
In order to study their action or to develop them as therapeutic agents, therefore, they must be delivered to the inside of the cell. This can be extremely difficult in the case of some bioactive peptides because of their inability to cross lipid membranes. Several strategies such as microinjection, liposome formation and electroporation have been used with varying degrees of success. In the past two years, however, two extraordinary discoveries have opened up new possibilities for peptide delivery. More exciting still was the discovery that they were capable of transporting into the cell covalently attached cargo such as peptide nucleic acids, and antisense oligonucleotides.