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


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. Study holds ProTherm entries: 10388, 10389 Extra Details: homeodomain; circular dichroism; transcription factor; DNA binding;,protein strucure; alpha-helix

Submission Details

ID: gXWeKVBT4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:40 p.m.

Version: 1

Publication Details
Damante G;Tell G;Leonardi A;Fogolari F;Bortolotti N;Di Lauro R;Formisano S,FEBS Lett. (1994) Analysis of the conformation and stability of rat TTF-1 homeodomain by circular dichroism. PMID:7957942
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