지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국자기공명학회 Journal of the Korean Magnetic Resonance Society Journal of the Korean Magnetic Resonance Society 제15권 제2호
- 발행연도
- 2011.1
- 수록면
- 137 - 145 (9page)
이용수
초록· 키워드
오류제보하기
Hsp33, a prokaryotic molecular chaperone, exerts holdase activity in response to oxidative stress. In this study, the stepwise conformational change of Hsp33 upon oxidation was monitored by NMR. In order to overcome its high molecular weight (33 kDa as a monomer and 66 kDa as a dimer), spectra were simplified using a selectively [^(15)N]His-labeled protein. All of the eight histidines were observed in the TROSY spectrum of the reduced Hsp33. Among them, three peaks showed dramatic resonance shifts dependent on the stepwise oxidation, indicating a remarkable conformational change. The results suggest that unfolding of the linker domain is associated with dimerization, but not entire region of the linker domain is unfolded.
목차
등록된 정보가 없습니다.
참고문헌 (14)
참고문헌 신청
Dae-Won Sim / 2009 / Backbone NMR assignments of a putative secretory protein from Helicobacter pylori, using ahigh - field (900MHz) NMR / Journal of the Korean Magnetic Res
I. Janda / 2004 / / Structure 12 : 1901 ~
J. Graumann / 2001 / / Structure 9 : 377 ~
J. Vijayalakshmi / 2001 / / Structure 9 : 367 ~
L. Jaroszewski / 2005 / / Proteins 61 : 669 ~
I. Janda / 2004 / / Structure 12 : 1901 ~
J. Graumann / 2001 / / Structure 9 : 377 ~
J. Vijayalakshmi / 2001 / / Structure 9 : 367 ~
L. Jaroszewski / 2005 / / Proteins 61 : 669 ~
이 논문의 저자 정보
최근 본 자료
댓글(0)
0