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
ID: gXWeKVBT4
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:40 p.m.
Version: 1
Number of data points | 3 |
Proteins | Homeobox protein Nkx-2.1 ; Homeobox protein Nkx-2.1 |
Unique complexes | 1 |
Assays/Quantities/Protocols | Experimental Assay: Tm ; Experimental Assay: dG_H2O ; Experimental Assay: dG_H2O temp:25.0 C |
Libraries | Mutations for sequence MRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKAAQQ |
Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
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Percent Identity | Matching Chains | Protein | Accession | Entry Name |
---|---|---|---|---|
100.0 | Homeobox protein Nkx-2.1 | Q9EQM3 | NKX24_MOUSE | |
98.4 | Homeobox protein Nkx-2.1 | P97273 | TITF1_CAVPO | |
100.0 | Homeobox protein Nkx-2.1 | Q9H2Z4 | NKX24_HUMAN | |
100.0 | Homeobox protein Nkx-2.1 | P50220 | NKX21_MOUSE | |
100.0 | Homeobox protein Nkx-2.1 | P23441 | NKX21_RAT | |
100.0 | Homeobox protein Nkx-2.1 | P43698 | TITF1_CANLF | |
100.0 | Homeobox protein Nkx-2.1 | P43699 | NKX21_HUMAN |