Triple isotope-[13C, 15N, 2H] labeling and NMR measurements of the inactive, reduced monomer form of Escherichia coli Hsp33

원형식; 이유섭; 고현숙; 류경석; 전영호

추천

검색

자료유형: 학술저널

저자정보: 원형식 이유섭 고현숙 류경석 전영호

저널정보: 한국자기공명학회 Journal of the Korean Magnetic Resonance Society Journal of the Korean Magnetic Resonance Society 제14권 제2호

발행연도: 2010.1

수록면: 117 - 126 (10page)

이용수

📌

연구주제

📖

연구배경

🔬

연구방법

🏆

연구결과

초록· 키워드

오류제보하기

Hsp33 is a molecular chaperone achieving a holdase activity upon response to a dual stress by heat and oxidation. Despite several crystal structures available, the activation process is not clearly understood, because the structure inactive Hsp33 as its reduced, zinc-bound, monomeric form has not been solved yet. Thus, we initiated structural investigation of the reduced Hsp33 monomer by NMR. In this study, to overcome the high molecular weight (33 kDa), the protein was triply isotope-[13C, 15N, 2H]-labeled and its inactive, monomeric state was ensured. 2D-[1H, 15N]-TROSY and a series of triple resonance spectra could be successfully obtained on a high-field (900 MHz) NMR machine with a cryoprobe. However, under all of the different conditions tested, the number of resonances observed was significantly less than that expected from the amino acid sequence. Thus, a possible contribution of dynamic conformational exchange leading to a line broadening is suggested that might be important for activation process of Hsp33.

#Hsp33 #zinc-binding #inactive monomer #redox-switch #triple labeling #conformational exchange

참고문헌 (17)

참고문헌 신청

B. Odaert / 2002 / / J. Biol. Chem. 277 : 12375 ~

C. Kumsta / 2009 / / Biochemistry 48 : 4666 ~

C.M. Cremers / 2010 / / J. Biol. Chem. 285 : 11243 ~

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

E. Barbar / 1999 / / Biopolymers 51 : 191 ~

함께 읽어보면 좋을 논문

논문 유사도에 따라 DBpia 가 추천하는 논문입니다. 함께 보면 좋을 연관 논문을 확인해보세요!