DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | Choi, Byong-Seok | - |
dc.contributor.advisor | 최병석 | - |
dc.contributor.author | Sun, Dawei | - |
dc.contributor.author | 순 다웨 | - |
dc.date.accessioned | 2011-12-13T04:50:35Z | - |
dc.date.available | 2011-12-13T04:50:35Z | - |
dc.date.issued | 2006 | - |
dc.identifier.uri | http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=255267&flag=dissertation | - |
dc.identifier.uri | http://hdl.handle.net/10203/32039 | - |
dc.description | 학위논문(석사) - 한국과학기술원 : 화학과, 2006.2, [ 44 p. ] | - |
dc.description.abstract | ATRIP, the regulatory protein of ATR, exits as one stable complex with ATR in human cells. Recent studies showed that ATR-ATRIP complex was localized to sites of DNA damage through interaction between N-terminal of ATRIP and RPA-ssDNA. And coiled-coil domain of ATRIP was predicated to be essential for stabilization of ATR binding and accumulation of ATR-ATRIP at DNA lesions. To characterize the structural feature of ATRIP, coiled-coil domain and N-terminal of ATRIP were investigated by NMR and biological approaches. CD spectra of N-terminal of ATRIP reveal that the second structure of N-terminal of ATRIP is dominated by a “random coil” contribution and is absent of tertiary structure. The unstructured N-terminal of ATRIP is further confirmed by 2-D 1H-15N HSQC characterized with narrow spreaded resonance frequency for amide protons both in 15N and 1H regions. However, NMR titration experiment shows that the folding structure of N-terminal of ATRIP can not be induced upon addition with RPA-ssDNA. Additionally, apparent binding between N-terminal of ATRIP and RPA-ssDNA can not be observed by pull-down assay using Ni-NTA agarose and chemical cross-linking with EDC in vitro. Regarding to coiled-coil domain of ATRIP, CD spectra reveals that coiled-coil domain of ATRIP is contributed by highly α-helix. And $2-D^1H-^{15}N$ HSQC of coiled-coil domain of ATRIP is characterized in highly order oligomerization. Furthermore, the highly order oligomerization of coiled-coil domain of ATRIP is determined to be likely induced by the common oligomeric interaction between coiled-coil domain $(ATRIP_{108-139aa})$ and coiled-coil domain $(ATRIP_{169-217aa})$. | eng |
dc.language | eng | - |
dc.publisher | 한국과학기술원 | - |
dc.subject | ATRIP | - |
dc.subject | NMR | - |
dc.subject | RPA-ssDNA | - |
dc.title | NMR studies on the coiled-coil domain and RPA-ssDNA | - |
dc.title.alternative | ATRIP의 coiled-coil도메인과 RPA-ssDNA결합 도메인에관한 NMR 연구 | - |
dc.type | Thesis(Master) | - |
dc.identifier.CNRN | 255267/325007 | - |
dc.description.department | 한국과학기술원 : 화학과, | - |
dc.identifier.uid | 020044304 | - |
dc.contributor.localauthor | Choi, Byong-Seok | - |
dc.contributor.localauthor | 최병석 | - |
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