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. Author manuscript; available in PMC: 2009 Sep 6.

Published in final edited form as: J Mol Biol. 2007 Dec 4;376(3):736–748. doi: 10.1016/j.jmb.2007.11.075

(a) Temperature-induced denaturation of GF (solid line) and GFO (dotted line) peptides monitored by circular dichroism spectroscopy at 225 nm. Both peptides (1mg/ml) were dissolved in buffer containing 20 mM glycine, 150 mM NaCl and 0.6M GuHCl, pH 2.0. Inset shows wavelength scans for both peptides recorded at 0°C, with the characteristic maximum at 225 nm. All samples were run under the same standard conditions (average heating rate = 0.1°C/min) ³⁰.

(b) Temperature dependence of the excess partial molar heat capacity (heating rate = 1°C/min) for GF (solid line) and GFO (dotted line) peptides monitored by differential scanning calorimetry. The calorimetric enthalpy values shown in table 2 represent the integration of the peaks. Both peptides (1mg/ml) were dissolved in buffer containing 20 mM glycine, 150 mM NaCl and 0.6M GuHCl, pH 2.0.

(a) Temperature-induced denaturation of GF (solid line) and GFO (dotted line) peptides monitored by circular dichroism spectroscopy at 225 nm. Both peptides (1mg/ml) were dissolved in buffer containing 20 mM glycine, 150 mM NaCl and 0.6M GuHCl, pH 2.0. Inset shows wavelength scans for both peptides recorded at 0°C, with the characteristic maximum at 225 nm. All samples were run under the same standard conditions (average heating rate = 0.1°C/min) ³⁰.

(b) Temperature dependence of the excess partial molar heat capacity (heating rate = 1°C/min) for GF (solid line) and GFO (dotted line) peptides monitored by differential scanning calorimetry. The calorimetric enthalpy values shown in table 2 represent the integration of the peaks. Both peptides (1mg/ml) were dissolved in buffer containing 20 mM glycine, 150 mM NaCl and 0.6M GuHCl, pH 2.0.