ANALYSIS OF THE CONFORMATION AND STABILITY OF RAT TTF-1 HOMEODOMAIN BY CIRCULAR-DICHROISM

被引：22

作者：

DAMANTE, G

TELL, G

LEONARDI, A

FOGOLARI, F

BORTOLOTTI, N

DILAURO, R

FORMISANO, S

机构：

[1] UNIV UDINE, DIPARTIMENTO SCI & TECNOL BIOMED, I-33100 UDINE, ITALY

[2] USSL 7, ANAL CLIN LAB, I-33100 UDINE, ITALY

来源：

FEBS LETTERS | 1994年 / 354卷 / 03期

关键词：

HOMEODOMAIN; CIRCULAR DICHROISM; TRANSCRIPTION FACTOR; DNA BINDING; PROTEIN STRUCTURE; ALPHA-HELIX;

D O I：

10.1016/0014-5793(94)01145-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 degrees C and a Delta 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 alpha-helical content of TTF-1HD significally modifies its DNA-binding activity.

引用

页码：293 / 296

页数：4

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