|
KMID : 0624620160490090497
|
|
BMB Reports
2016 Volume.49 No. 9 p.497 ~ p.501
|
|
|
Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment
|
|
Tompa Peter
Han Kyou-Hoon
Bokor Monika
Kamasa Pawel
Tantos Agnes
Fritz Beata
Kim Do-Hyoung
Lee Che-Wook
Verebelyi Tamas
Tompa Kalman
|
|
|
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.
|
|
|
KEYWORD
|
|
|
Differential Scanning Calorimetry (DSC), Hydration, p53 Transactivation Domain (p53TAD), Pre-Structured Motif (PreSMo), Wide-line NMR
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|