Comparison with thermal unfolding

Thermal denaturation of CI2 at 353 K yields a stable and long-lived (>3.0 ns) intermediate structure with an rmsd(Ca) of 2.8 A with respect to the crystal structure, only 0.8 A greater than the control simulation of the native state at 298 K. This structure was native-like but expanded in comparison to the control simulation. Increasing the temperature of the denaturation run to 498 K causes the protein to unfold within only 600 ps to an rmsd(Ca) of approximately 12 A." It was desirable to apply a method for denaturing CI2 at lower temperature to avoid possible thermal problems without sacrificing the enhanced unfolding rates at higher temperatures. 

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