DC Field | Value | Language |
---|---|---|
dc.contributor.author | P Tompa | - |
dc.contributor.author | Kyou Hoon Han | - |
dc.contributor.author | M Bokor | - |
dc.contributor.author | P Kamasa | - |
dc.contributor.author | A Tantos | - |
dc.contributor.author | B Fritz | - |
dc.contributor.author | Do-Hyoung Kim | - |
dc.contributor.author | Chewook Lee | - |
dc.contributor.author | T Verebelyi | - |
dc.contributor.author | K Tompa | - |
dc.date.accessioned | 2017-04-19T10:30:15Z | - |
dc.date.available | 2017-04-19T10:30:15Z | - |
dc.date.issued | 2016 | - |
dc.identifier.issn | 1225-8687 | - |
dc.identifier.uri | 10.5483/BMBRep.2016.49.9.037 | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/13555 | - |
dc.description.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. | - |
dc.publisher | Korea Soc-Assoc-Inst | - |
dc.title | Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment | - |
dc.title.alternative | Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment | - |
dc.type | Article | - |
dc.citation.title | BMB Reports | - |
dc.citation.number | 9 | - |
dc.citation.endPage | 501 | - |
dc.citation.startPage | 497 | - |
dc.citation.volume | 49 | - |
dc.contributor.affiliatedAuthor | Kyou Hoon Han | - |
dc.contributor.affiliatedAuthor | Do-Hyoung Kim | - |
dc.contributor.affiliatedAuthor | Chewook Lee | - |
dc.contributor.alternativeName | Tompa | - |
dc.contributor.alternativeName | 한규훈 | - |
dc.contributor.alternativeName | Bokor | - |
dc.contributor.alternativeName | Kamasa | - |
dc.contributor.alternativeName | Tantos | - |
dc.contributor.alternativeName | Fritz | - |
dc.contributor.alternativeName | 김도형 | - |
dc.contributor.alternativeName | 이제욱 | - |
dc.contributor.alternativeName | Verebelyi | - |
dc.contributor.alternativeName | Tompa | - |
dc.identifier.bibliographicCitation | BMB Reports, vol. 49, no. 9, pp. 497-501 | - |
dc.identifier.doi | 10.5483/BMBRep.2016.49.9.037 | - |
dc.subject.keyword | Differential Scanning Calorimetry (DSC) | - |
dc.subject.keyword | Hydration | - |
dc.subject.keyword | P53 Transactivation Domain (p53TAD) | - |
dc.subject.keyword | Pre-Structured Motif (PreSMo) | - |
dc.subject.keyword | Wide-line NMR | - |
dc.subject.local | Differential Scanning Calorimetry (DSC) | - |
dc.subject.local | Hydration | - |
dc.subject.local | hydration | - |
dc.subject.local | P53 Transactivation Domain (p53TAD) | - |
dc.subject.local | p53 transactivation domain | - |
dc.subject.local | PreSMos (Pre-Structured Motifs) | - |
dc.subject.local | Pre-structured motif | - |
dc.subject.local | Prestructured motif (PreSMo) | - |
dc.subject.local | Pre-structured motif (PreSMo) | - |
dc.subject.local | PreSMo (Pre-Structured Motif) | - |
dc.subject.local | pre-structured motif | - |
dc.subject.local | pre-structured motifs (PreSMos) | - |
dc.subject.local | Pre-Structured Motif (PreSMo) | - |
dc.subject.local | PreSMo | - |
dc.subject.local | PreSMos (pre-structured motifs) | - |
dc.subject.local | Wide-line NMR | - |
dc.description.journalClass | Y | - |
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