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. 2007 May 2;129(17):5374-5.
doi: 10.1021/ja0714538. Epub 2007 Apr 6.

Unbiased cold denaturation: low- and high-temperature unfolding of yeast frataxin under physiological conditions

Annalisa Pastore  1 , Stephen R Martin, Anastasia Politou, Kalyan C Kondapalli, Timothy Stemmler, Piero A Temussi
Affiliations

Unbiased cold denaturation: low- and high-temperature unfolding of yeast frataxin under physiological conditions

Annalisa Pastore et al. J Am Chem Soc. .
No abstract available

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Figures

Figure 1
Figure 1
Representative NMR spectra of Yfh1 in the temperature range −5 to 45 °C: (A) 15N-1H HSQC correlation spectra of Yfh1 in 20 mM HEPES at pH 7.0 at three representative temperatures; (B) high field portions of 1D spectra of Yfh1 in 20 mM HEPES at pH 7.0 at seven representative temperatures. The sample used for quantitative measurements was extensively dialyzed and contains TSP for reference (0 ppm) and calibration.
Figure 2
Figure 2
Plots of NMR and CD signals of Yfh1 as a function of temperature. Relative integrals of the highest field peaks of Yfh1 in HEPES at pH 7.0 are shown as circles (right-hand side scale). Far UV absorbance in the CD spectra of Yfh1 in 20 mM Tris at pH 7.5 corresponds to the left-hand side scale.
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