| Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment |
| Peter Tompa1,#, Kyou-Hoon Han2,3,*,#, Monika Bokor4, Pawel Kamasa4, Agnes Tantos1, Beata Fritz1, Do-Hyoung Kim2, Chewook Lee2, Tamas Verebelyi4, Kalman Tompa4 |
1Institute of Enzymology, Hungarian Academy of Sciences,
2Genome Editing Research Center, Korea Research Institute of Bioscience and Biotechnology,
3Department of Nano & Bioinformatics, University of Science and Technology,
4Institute for Solid State Physics and Optics, Hungarian Academy of Sciences |
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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 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 in order to characterize their water and ion binding characteristics. By quantifying the number of hydrate water molecules, we provide 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 also are able to bind a larger amount of charged solute ions.
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| Abstract, Accepted Manuscript(in press) [Submitted on February 24, 2016, Accepted on March 26, 2016] |
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