title: Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.
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. [BMB Reports 2016; 49(9): 497-501].
authors.affiliation: Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest 1117, Hungary.
authors.forename: Peter
authors.initials: P
authors.lastname: Tompa
authors.affiliation: Genome Editing Research Center, Division of Biomedical Science, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141; Department of Nano & Bioinformatics, University of Science and Technology (UST), Daejeon 34113, Korea.
authors.forename: Kyou-Hoon
authors.initials: KH
authors.lastname: Han
authors.affiliation: Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences, Budapest H-1525, Hungary.
authors.forename: Mónika
authors.initials: M
authors.lastname: Bokor
authors.affiliation: Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences, Budapest H-1525, Hungary.
authors.forename: Pawel
authors.initials: P
authors.lastname: Kamasa
authors.affiliation: Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest 1117, Hungary.
authors.forename: Ágnes
authors.initials: Á
authors.lastname: Tantos
authors.affiliation: Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest 1117, Hungary.
authors.forename: Beáta
authors.initials: B
authors.lastname: Fritz
authors.affiliation: Genome Editing Research Center, Division of Biomedical Science, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Korea.
authors.forename: Do-Hyoung
authors.initials: DH
authors.lastname: Kim
authors.affiliation: Genome Editing Research Center, Division of Biomedical Science, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141.
authors.forename: Chewook
authors.initials: C
authors.lastname: Lee
authors.affiliation: Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences, Budapest H-1525, Hungary.
authors.forename: Tamás
authors.initials: T
authors.lastname: Verebélyi
authors.affiliation: Institute for Solid State Physics and Optics, Wigner Research Centre for Physics, Hungarian Academy of Sciences, Budapest H-1525, Hungary.
authors.forename: Kálmán
authors.initials: K
authors.lastname: Tompa
mesh_terms: D002152:Calorimetry, Differential Scanning; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D012965:Sodium Chloride / Q000737:chemistry; D013696:Temperature; D015533:Transcriptional Activation; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D014867:Water / Q000737:chemistry
chemical_list: D011994:Recombinant Proteins; D016159:Tumor Suppressor Protein p53; D014867:Water; D012965:Sodium Chloride