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The CD spectroscopy of biomolecules is described. The challenges faced in carrying out the analysis of these spectra, due to the many chromophores contained within large biomolecules, are outlined. Examples of the use of the CD technique to derive qualitative information from changes in the folding of protein molecules are provided. The use of distinctive CD spectra associated with α-helix, β-sheet, β-turn and random coil structure types within proteins to estimate the percentage of each is outlined.

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