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  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Characterizing early oligomerization of Ab42 to understand Alzheimer amyloid aggregation process

등록일
2008년 8월 11일 18시 05분 02초
접수번호
0754
발표코드
금15J4심 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 16시 : 00분
발표형식
심포지엄
발표분야
생명화학 - Omics & Personalized Medicine II
저자 및
공동저자
함시현
숙명여자대학교 화학과, Korea
The amyloid beta (Ab) proteins are responsible for amyloid plaques in Alzheimer’s disease and have been the most widely studied subject in the process of fibril growth. Although much progress has been made to elucidate amyloid fibril properties at a molecular level, the full identification and characterization of all the conformational states and oligomeric structures in the aggregation process and all the conformational changes that link between those different states are still needed to be revealed. Here, we present long time all-atom molecular dynamics (MD) simulations in explicit water to investigate the structural and dynamical aspects of full-length Ab(1-42) Alzheimer’s disease protein. By performing the Ab(1-42) monomer and oligomers simulations, we investigated the driving forces and the structural motif of the oligomerization process and the structural and dynamic characterization of amyloid beta protein from our MD results may provide an important key factor to both therapeutic and prevention of Alzheimer’s disease.

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