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
收藏
页码:293 / 296
页数:4
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