Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment
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Tartalom: http://real.mtak.hu/39832/
Archívum: MTA Könyvtár
Gyűjtemény: Status = Published

Type = Article
Cím:
Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment
Létrehozó:
Tompa, PĂŠter
Han, Kyou-Hoon
Bokor, MĂłnika
Kamasa, Pawel
Tantos, Ágnes
Fritz, BeĂĄta
Kim, Do-Hyoung
Lee, Chewook
VerebĂŠlyi, TamĂĄs
Tompa, KĂĄlmĂĄn
Kiadó:
The Korean Society for Biochemistry and Molecular Biology
Dátum:
2016-04-04
Téma:
QH301 Biology / biolĂłgia
Tartalmi leírás:
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.
Nyelv:
angol
magyar
Típus:
Article
PeerReviewed
info:eu-repo/semantics/article
Formátum:
text
text
Azonosító:
Tompa, PÊter and Han, Kyou-Hoon and Bokor, Mónika and Kamasa, Pawel and Tantos, Ágnes and Fritz, Beåta and Kim, Do-Hyoung and Lee, Chewook and VerebÊlyi, Tamås and Tompa, Kålmån (2016) Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment. BMB reports, 49 (9). pp. 497-501. ISSN 1976-670X
Kapcsolat:
MTMT:3131028; doi:10.5483/BMBRep.2016.49.9.037