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

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dc.contributor.authorP Tompa-
dc.contributor.authorKyou Hoon Han-
dc.contributor.authorM Bokor-
dc.contributor.authorP Kamasa-
dc.contributor.authorA Tantos-
dc.contributor.authorB Fritz-
dc.contributor.authorDo-Hyoung Kim-
dc.contributor.authorChewook Lee-
dc.contributor.authorT Verebelyi-
dc.contributor.authorK Tompa-
dc.date.accessioned2017-04-19T10:30:15Z-
dc.date.available2017-04-19T10:30:15Z-
dc.date.issued2016-
dc.identifier.issn1225-8687-
dc.identifier.uri10.5483/BMBRep.2016.49.9.037ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13555-
dc.description.abstractWide-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.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleWide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment-
dc.title.alternativeWide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment-
dc.typeArticle-
dc.citation.titleBMB Reports-
dc.citation.number9-
dc.citation.endPage501-
dc.citation.startPage497-
dc.citation.volume49-
dc.contributor.affiliatedAuthorKyou Hoon Han-
dc.contributor.affiliatedAuthorDo-Hyoung Kim-
dc.contributor.affiliatedAuthorChewook Lee-
dc.contributor.alternativeNameTompa-
dc.contributor.alternativeName한규훈-
dc.contributor.alternativeNameBokor-
dc.contributor.alternativeNameKamasa-
dc.contributor.alternativeNameTantos-
dc.contributor.alternativeNameFritz-
dc.contributor.alternativeName김도형-
dc.contributor.alternativeName이제욱-
dc.contributor.alternativeNameVerebelyi-
dc.contributor.alternativeNameTompa-
dc.identifier.bibliographicCitationBMB Reports, vol. 49, no. 9, pp. 497-501-
dc.identifier.doi10.5483/BMBRep.2016.49.9.037-
dc.subject.keywordDifferential Scanning Calorimetry (DSC)-
dc.subject.keywordHydration-
dc.subject.keywordP53 Transactivation Domain (p53TAD)-
dc.subject.keywordPre-Structured Motif (PreSMo)-
dc.subject.keywordWide-line NMR-
dc.subject.localDifferential Scanning Calorimetry (DSC)-
dc.subject.localHydration-
dc.subject.localhydration-
dc.subject.localP53 Transactivation Domain (p53TAD)-
dc.subject.localp53 transactivation domain-
dc.subject.localPreSMos (Pre-Structured Motifs)-
dc.subject.localPre-structured motif-
dc.subject.localPrestructured motif (PreSMo)-
dc.subject.localPre-structured motif (PreSMo)-
dc.subject.localPreSMo (Pre-Structured Motif)-
dc.subject.localpre-structured motif-
dc.subject.localpre-structured motifs (PreSMos)-
dc.subject.localPre-Structured Motif (PreSMo)-
dc.subject.localPreSMo-
dc.subject.localPreSMos (pre-structured motifs)-
dc.subject.localWide-line NMR-
dc.description.journalClassY-
Appears in Collections:
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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