Analysis of the conformation and stability of rat TTF‐1 homeodomain by circular dichroism

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Abstract
The conformational stability of TTF‐1HD has been determined by CD‐monitored thermal denaturation and isothermal urea unfolding studies. The Gibbs free energy of stabilization found are 1.44 and 1.26 kcal·mol−1, respectively. TTF‐1HD exhibits a T m of 42°C and a δC p of 80 cal·mol−1·K−1 indicating that TTF‐1HD, when free in solution, is a mobile flexible segment folded into loose helices. Such a flexibility would be relevant for the DNA‐binding function of this homeodomain. In fact, a small reduction of the α‐helical content of TTF‐1HD significally modifies its DNA‐binding activity.