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. Author manuscript; available in PMC: 2010 Jul 13.
Published in final edited form as: J Biol Chem. 2004 Jul 1;279(43):44841–44846. doi: 10.1074/jbc.M406257200

FIG. 5. Influence of urea on the EPR Spectrum of vimentin spin labeled at residue 333 of rod domain 2.

FIG. 5

This residue is predicted to occupy a “d” position in the heptad and thus to serve as an indicator of both α helix formation and coiled coil formation. Spectra of assembly intermediates were taken from samples harvested during stepwise dialysis, and are normalized for the protein concentration in each sample. The concentration of urea at which the spectrum was taken is indicated in the figure.