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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국자기공명학회 Journal of the Korean Magnetic Resonance Society Journal of the Korean Magnetic Resonance Society 제21권 제1호
- 발행연도
- 2017.1
- 수록면
- 13 - 19 (7page)
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Human sterol Δ8-Δ7 isomerase, commonly known as emopamil binding protein (EBP), is an essential protein in the cholesterol-synthetic pathway, and mutations of this protein are critically associated with human diseases such as Conradi-Hunermann–Happle or male EBP disorder with neurological defects syndrome. Due to such a clinical importance, EBP has been intensively investigated and some important features have been reported. EBP is a tetra-spanning membrane protein, of which 2nd, 3rd, and 4th membrane-spanning α helices play an important role in its enzymatic function. However, detailed structural feature at atomic resolution has not yet been elucidated, due to characteristic difficulties in dealing with membrane protein. Here, we over-expressed EBP using Escherichia coli and performed detergent screening to find suitable membrane mimetics for structural studies of the protein by NMR. As results, DPC and LMPG could be evaluated as the most favorable detergents to acquire promising NMR spectra for structural study of EBP.
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