Protein folding intermediates, circular dichroism

R. W. Woody, Circular Dichroism of Protein-Folding Intermediates , in Methods in Enzymology, eds. J. Holt, M. Johnson and G. Ackers, Elsevier, 2004, vol. 380, Energetics of Biological Macromolecules, Part E, p. 242. 

FIGURE 11.15 Resolution of the protein folding of a-apolactalbumin. (a) Detection of changes in protein secondary structure (far-UV circular dichroism measurements), (b) Detection of changes in protein tertiary structure (near-UV circular dichroism measurements), (c) Complete description of protein folding. Resolution of the row-wise data set formed by near-UV (Dj) and far-UV (D2) circular dichroism measurements. Solid line native conformation, dash-dotted line intermediate conformation, dotted line unfolded conformation. 

Navea, S., de Juan, A., and Tauler, R., Detection and resolution of intermediate species in protein folding processes using fluorescence and circular dichroism spectroscopies and multivariate curve resolution, Anal. Chem., 64, 6031-6039, 2002. 

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