Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics

Recent developments in instrumentation and bioinformatics show that the tec hnique of synchrotron radiation circular dichroism spectroscopy can provide novel information on protein secondary structures and folding motifs, and has the potential to play an important role in structural genomics studies, both as a means of target selection and as a high-throughput, low-sample-r equiring screening method. This is possible because of the additional infor mation content in the low-vacuum ultraviolet wavelength data obtainable wit h intense synchrotron radiation light sources, compared with that present i n spectra from conventional lab-based circular dichroism instruments.