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. Author manuscript; available in PMC: 2012 May 4.
Published in final edited form as: J Am Chem Soc. 2011 Apr 6;133(17):6681–6691. doi: 10.1021/ja111009s

Figure 5.

Figure 5

The temperature dependence of the linewidth of the native peak (A) and the unfolded peak (B) of the protein CO spectrum. The increase in width of the unfolded spectra with increasing temperature is caused by an increase in the inhomogeneous contribution, which results from an increase in the number of protein structures. The change in width with temperature demonstrates that the temperature dependent unfolding is not a two state process. C and D show the temperature dependence of the center frequency for the native and unfolded peaks, respectively. As with the FWHM, the native peak frequency shows little change, but the unfolded peak displays a discernable dependence on temperature. The error are from the errors in fitting the spectra at each temperature. Because there is only a small population of the native protein (blue points) at higher temperatures, the error bars are larger. Conversely, data for the unfolded protein (red points) have larger error bars at lower temperatures.