| Literature DB >> 7957942 |
G Damante1, G Tell, A Leonardi, F Fogolari, N Bortolotti, R Di Lauro, S Formisano.
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 Tm of 42 degrees C and a delta Cp 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 alpha-helical content of TTF-1HD significantly modifies its DNA-binding activity.Entities:
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Year: 1994 PMID： 7957942 DOI： 10.1016/0014-5793(94)01145-1
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124