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  • 02월 22일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Expression, Isotope Labeling, and Purification of a Transmembrane Region of Human Amyloid-β Protein in Escherichia coli for Solid-state NMR Studies

등록일
2008년 2월 14일 12시 36분 11초
접수번호
1360
발표코드
31P67포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅱ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
박태준, 임수연, 김용애
한국외국어대학교 화학과,
Enormous progress has been made towards understanding of the cell biology and plaque properties of Alzheimer’s disease. But globular and nonfibrillar Amyloid-β proteins are continuously produced during normal cellular metabolism and are also present in Alzheimer tissues. In addition to it, small nonfibrillar Amyloid-β protein alone is sufficient to cause cellular degradation. One of the possible mechanisms for Amyloid-β protein toxicity suggests that nonfibrillar Amyloid-β protein form calcium-permeable ion channels in the cell plasma membrane. These channels might allow excessive calcium influx and disrupt the normal cellular calcium homeostasis. But little is known about the transmembrane region and the channel structure of Amyloid-β protein as an ion-channel protein as yet except theoretical model. We will elucidate the channel structure and mechanisms of their formation that is critical for developing therapeutic agents. Here, we report high-yield expression and purification of a transmembrane peptide of the Amyloid -β protein. And we will also present solid-state NMR structural studies of aligned samples of transmembrane protein.

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