FEBS Letters | |
Analysis of the conformation and stability of rat TTF‐1 homeodomain by circular dichroism | |
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
【 预 览 】
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