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
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:40 p.m.
|Number of data points||3|
|Proteins||Homeobox protein Nkx-2.1 ; Homeobox protein Nkx-2.1|
|Assays/Quantities/Protocols||Experimental Assay: Tm ; Experimental Assay: dG_H2O ; Experimental Assay: dG_H2O temp:25.0 C|
|Libraries||Mutations for sequence MRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKAAQQ|