Premium
Analysis of the conformation and stability of rat TTF‐1 homeodomain by circular dichroism
Author(s) -
Damante Giuseppe,
Tella Gianluca,
Leonardi Antonio,
Fogolari Federico,
Bortolotti Nadia,
Di Lauroa Roberto,
Formisano Silvestro
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01145-1
Subject(s) - circular dichroism , gibbs free energy , chemistry , crystallography , denaturation (fissile materials) , thermal stability , thermodynamics , physics , organic chemistry , nuclear chemistry
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 δ C 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.