The main aim of my research is to gain an understanding of protein function at a molecular level from investigations of protein structure employing single crystal X-ray diffraction. Together with other complementary methodologies such as CD and NMR spectroscopy, calorimetry, chromatography and mutagenesis procedures and collaboration with experts in the wider biomedical perspective of each protein we endeavour to exploit this detailed knowledge. Binding sites for small molecule ligands are targets for drug development. Enzyme active sites can be modified to catalyse novel reactions. Protein quaternary structure can be modified to provide new materials. Research on the structure and function of the pentraxin proteins C-reactive protein (CRP) and serum amyloid P component (SAP) have peaked in prominence recently in the context of the development of antagonists with therapeutic potential. SAP is a protein that decorates amyloid deposits both in systemic disease and in neurodegenerative diseases. It attaches to fibrous deposits of A?1-42, prion and tau as well as a host of other fibre proteins. Targeting this interaction with antagonists is a promising route to treatments for these otherwise essentially untreatable diseases. For C-reactive protein, we have good evidence that our designed antagonists are cardio and neuroprotective following heart attacks or strokes. Our work has established a novel mode of drug action whereby two pharmacophores are presented on each drug molecule, driving enhanced affinity and target crosslinking. The cross-linked target proteins are cleared rapidly by the liver. This approach will find wide application.