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

FEBS Letters

Leonardi, Antonio²  Damante, Giuseppe²  Fogolari, Federico²  Bortolotti, Nadia¹  Di Lauroa, Roberto²  Formisano, Silvestro²  Tella, Gianluca² 

[1] Laboratorio di Analisi Cliniche USSL 7, Istituto Gervasutta, Via Gervasutta 48, 33100 Udine, Italy;Dipartimento di Scienze e Tecnologie Biomediche, Università degli Studi di Udine, Via Gervasutta 48, 33100 Udine, Italy

关键词: Homeodomain;    Circular dichroism;    Transcription factor;    DNA binding;    Protein structure;    α-Helix;    TTF-1HD;    thyroid transcription factor 1 homeodomain;    CD;    circular dichroism;   

DOI  :  10.1016/0014-5793(94)01145-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown