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  • 09월 04일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Multifarious effort for optimization of expression, purification, and structural characterization of disease related human transmembrane proteins

2014년 8월 28일 16시 58분 04초
PHYS.P-468 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 15일 (수요일) 16:00~19:00
저자 및
김지선, 김경섭, 김용애*
한국외국어대학교 화학과, Korea
Human transmembrane proteins (hTMPs) are closely related to transport, channel formation, signaling, cell to cell interaction, so they are the crucial target of modern medicinal drugs. In order to study the structure and function of these hTMPs, it is important to prepare reasonable amounts of proteins. However their preparation is seriously difficult and time-consuming due to insufficient yields and low solubility of hTMPs. We tried to produce large amounts of human amyloid-β (hA?? that is related to the dementia and human melanocortin-4 receptor (hMC4R) that is related to the severe early onset obesity. The hA? transmembrane protein shows membrane-bound oligomeric state, and the Ca2+-permeable ion channel formation of non-fibril in the cell membrane. It plays a central role in pathogenesis of dementia and Alzheimer disease. The hMC4R has a critical role in part of energy homeostasis like the food intake and energy consumption. Heterozygous mutation D90N located in second transmembrane domain of hMC4R relate in genetic cause of human obesity. In this research, we succeed to produce the trans-membrane domain of the hAβ and second trans-membrane domain both of the wild-type hMC4R (wt-TM2) and mutant hMC4R (m-TM2). To assess the structural characterizations of these proteins in the membrane-like environments, we were obtained enough quantities of proteins by using a recombinant DNA technology and highly purified proteins were applied to a few biophysical analysis techniques like PAGE, CD, MS, solution and solid-state NMR spectroscopy. In addition, we could get 1H-15N 1D, 2D SAMMY and SMAPI spectra using home-built solid-state NMR probe.