Fold recognition by synchrotron radiation circular dichroism spectroscopy: a new tool for structural proteomics and structural molecular biology

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The three dimensional structures of proteins define their functional properties. At the present time, circular dichroism spectroscopic methods can be used to examine the structures of proteins in solution at the level of secondary (local) structure. This proposal is to develop a new methodology to extend the information content using lower wavelength data. Such a method will provide complementary informtion to that produced by new programmes in structural proteomics being developed in the UK and abroad, especially as it will provide structural information at the level of architecture and fold motifs to be derived from very small amounts of proteins, including those that do not crystallise. In addition, as the UK has invested in a new third-generation synchrotron light source, Diamond, which will have a circular dichroism station as one of its early beamlines, this proposal will provide a new application and means of extracting extra information from the data collected on that beamline.