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• W2495372721 abstract "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." @default.
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• W2495372721 date "2016-09-30" @default.
• W2495372721 modified "2023-09-30" @default.
• W2495372721 title "Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment" @default.
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• W2495372721 doi "https://doi.org/10.5483/bmbrep.2016.49.9.037" @default.
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