|Title||Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.|
|Publication Type||Journal Article|
|Year of Publication||2016|
|Authors||Tompa, P., Han K-H., Bokor M., Kamasa P., Tantos Á., Fritz B., Kim D-H., Lee C., Verebélyi T., and Tompa K.|
|Date Published||2016 Sep|
Wide-line 1H NMR intensity and differential scanning calorimetry measurements were carried out on the intrinsically disordered 73-residue full transactivation domain (TAD) of the p53 tumor suppressor protein and two peptides: one a wild type p53 TAD peptide with a helix pre-structuring property, and a mutant peptide with a disabled helix-forming propensity. Measurements were carried out in order to characterize their water and ion binding characteristics. By quantifying the number of hydrate water molecules, we provide a microscopic description for the interactions of water with a wild-type p53 TAD and two p53 TAD peptides. The results provide direct evidence that intrinsically disordered proteins (IDPs) and a less structured peptide not only have a higher hydration capacity than globular proteins, but are also able to bind a larger amount of charged solute ions. [BMB Reports 2016; 49(9): 497-501].
|Alternate Journal||BMB Rep|
Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.