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

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Title
Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment
Author(s)
P Tompa; Kyou Hoon Han; M Bokor; P Kamasa; A Tantos; B Fritz; Do-Hyoung Kim; Chewook Lee; T Verebelyi; K Tompa
Bibliographic Citation
BMB Reports, vol. 49, no. 9, pp. 497-501
Publication Year
2016
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.
Keyword
Differential Scanning Calorimetry (DSC)HydrationP53 Transactivation Domain (p53TAD)Pre-Structured Motif (PreSMo)Wide-line NMR
ISSN
1225-8687
Publisher
Korea Soc-Assoc-Inst
DOI
http://dx.doi.org/10.5483/BMBRep.2016.49.9.037
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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