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http://dx.doi.org/10.5483/BMBRep.2016.49.9.037

Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment  

Tompa, Peter (Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences)
Han, Kyou-Hoon (Genome Editing Research Center, Division of Biomedical Science, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Bokor, Monika (Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences)
Kamasa, Pawel (Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences)
Tantos, Agnes (Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences)
Fritz, Beata (Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences)
Kim, Do-Hyoung (Genome Editing Research Center, Division of Biomedical Science, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Lee, Chewook (Genome Editing Research Center, Division of Biomedical Science, Korea Research Institute of Bioscience and Biotechnology (KRIBB))
Verebelyi, Tamas (Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences)
Tompa, Kalman (Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences)
Publication Information
BMB Reports / v.49, no.9, 2016 , pp. 497-501 More about this Journal
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.
Keywords
Differential Scanning Calorimetry (DSC); Hydration; p53 Transactivation Domain (p53TAD); Pre-Structured Motif (PreSMo); Wide-line NMR;
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