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학술발표회초록보기

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  • 09월 08일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제116회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Probing Structural Dynamics of Intrinsically Disordered Amyloid Proteins using SAXS Spectroscopy and Ion Mobility Mass Spectrometry

등록일
2015년 8월 27일 22시 07분 52초
접수번호
1090
발표코드
ANAL2-2 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
금 09시 : 20분
발표형식
심포지엄
발표분야
분석화학 - Material Sciences in Analytical Chemistry
저자 및
공동저자
김준곤
고려대학교 화학과, Korea
Information of structural dynamics and interactions of intrinsically disordered amyloid proteins is quite limited despite its importance to establish a principle for developing therapeutics for the associated degenerative diseases. Electrospray ionization ion mobility mass spectrometry (ESI-IM-MS) has been successfully applied to assess the structural analysis of proteins with its unique ability to separate, isolate, and characterize each conformer of protein. However, correlation between the structures of proteins in the gas phase and in solution has been yet to be understood clearly. In our laboratory, we have been utilized synchrotron solution small angle X-ray scattering (SAXS) spectroscopy and ESI-IM-MS for identification of conformers of intrinsically disordered proteins (IDPs) in solution and the gas phase, respectively. In this presentation, I will discuss our approach for characterizing the conformational dynamics and intermolecular interactions of IDPs using these two techniques. For example, beta-amyloid peptide (Ab) undergoes complexation with human serum albumin (HSA). We probed specific binding sites of Ab1-40 in HSA and structural conversion of Ab1-40 upon complexation. Additional examples of structural dynamics and aggregations of amyloid proteins will be further discussed.

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