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  • 09월 20일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제126회 대한화학회 학술발표회 및 총회 An integrated approach for probing quaternary structure change of protein induced by ligand using SAXS and cross-linking/MS

등록일
2020년 9월 10일 14시 45분 52초
접수번호
1283
발표코드
ANAL2.O-13 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
화 10시 : 48분
발표형식
구두발표
발표분야
Analytical Chemistry - Oral Presentation of Young Analytical Chemists II
저자 및
공동저자
Chae Eun Heo, Chae Ri Park, MyungKook Son, Dongjoon Im, Sooyeon Chae, Minji Kim1, Hugh I. Kim*
Department of Chemistry, Korea University, Korea
1Chemistry Department of Nano-Science, Ewha Womans University, Korea
Characterization of the protein-protein interactions is crucial for the study of a wide variety of biological systems. Numerous research has been reported that various methods are developed to support the identification, characterization, and analysis of protein complexes. Since the protein-protein interactions are easily influenced by post-translational modification (PTM), metal ions, and ion concentration, the development of methods to probe protein-protein interaction induced by environmental factors is needed. Here, we have investigated the ATP effect on the quaternary structure of insulin using multiple biophysical analyses. Firstly, we have conducted the solution small-angle X-ray scattering (SAXS) experiments to understand insulin overall size information, protein association state from their scattering profiles. Then, to identify, characterize, and quantify intermolecular protein-protein interactions in the presence and absence of ATP, we performed crosslinking-mass spectrometry (XL-MS) using two crosslinkers. Finally, we executed molecular docking simulation using our obtained information from the XL-MS regarding residue-residue interaction, and simulated structures were compared to the experimental SAXS profiles to suggest possible protein structures. The experimental methodology using diverse analytical techniques would be highly helpful in understanding the protein-protein interactions.

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