Abstract
To elucidate the contribution of tryptophan side chains to the vacuum-ultraviolet (VUV) circular dichroism (CD) of Escherichia coli dihydrofolate reductase, we measured the VUVCD spectra of eight tryptophan mutants down to 175nm. The difference spectra between the wild-type and the mutants clearly demonstrated that the contribution of tryptophan side chains extends to the high-energy peptide CD in the VUV region. These results should be useful for a theoretical study on improving protein secondary-structure analysis by VUVCD spectroscopy.
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