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  • 09월 05일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제120회 대한화학회 학술발표회, 총회 및 기기전시회 안내 The structural characterization of disease related human transmembrane proteins using the NMR spectroscopy

등록일
2017년 8월 24일 16시 45분 26초
접수번호
3120
발표코드
ANAL2.O-23 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 10시 : 05분
발표형식
구두발표
발표분야
Analytical Chemistry - Oral Presentation of Young Analytical Chemists II
저자 및
공동저자
Seongjin Cho, Ji Sun Kim, YONGAE KIM*
Department of Chemistry, Hankuk University of Foreign Studies, Korea
Human transmembrane proteins (hTMPs) play essential roles in cellular metabolism, participating in processes such as ion transport, nutrient uptake, signal transduction, and intercellular communication. However, aggregation or misfolding of hTMPs due to unwanted mutations of amino acid sequences or errors in the folding process leads to an increase in various human diseases. Therefore, we aim to create new treatments that can inhibit or eliminate these changes. In this research, we tried to identify the structure of human amyloid-β (hAβ) and human melanocortin-4 receptor (hMC4R). The hAβ transmembrane protein shows that the non-fibrillar hAβs form the Ca2+-permeable ion channel in the cell membrane and these channels can disrupt the normal cellular calcium homeostasis. It plays an important role in pathogenesis of dementia and Alzheimer disease. The human melanocortin-4 receptor (hMC4R) has been highlighted because it is central regulator of body weight. Heterozygous mutations related in genetic cause of severe obesity. We succeed to produce the transmembrane domain of the hAβ and second transmembrane domain of the wild-type hMC4R and mutant hMC4R. In cases of the wt/m-TM2 purification, we used sodium dodecyl sulfate (SDS) because of their hydrophobicity. Since SDS binds so strongly to protein, it interferes with biophysical techniques used for characterization of wt/m TM2. Thus, we developed the removal methods of SDS to obtain high quality of purification for wt/m-TM2. Highly purified proteins were applied to several analysis techniques like PAGE, CD, MASS, solution and solid-state NMR spectroscopy. In addition, we could get 1H-15N 1D, 2D SAMMY and SAMPI spectra using home-built solid-state NMR probe.

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