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Title 

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

Authors 

P TompaKyou Hoon HanM BokorP KamasaA TantosB FritzDo-Hyoung KimChewook LeeT VerebelyiK Tompa

Publisher 

Korean Society for Biochemistry and Molecular Biology

Issue Date 

2016

Citation 

BMB Reports, vol. 49, no. 9, pp. 497-501

Keywords 

Differential Scanning Calorimetry (DSC)HydrationP53 Transactivation Domain (p53TAD)Pre-Structured Motif (PreSMo)Wide-line NMR

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.

ISSN 

1225-8687

Link 

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

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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