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제126회 대한화학회 학술발표회 및 총회 Elucidating Protein Topologies Using Ion Mobility-Mass Spectrometry: From String to Pretzelane

등록일
2020년 9월 9일 12시 28분 45초
접수번호
0911
발표코드
PHYS1-6 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
화 12시 : 30분
발표형식
심포지엄
발표분야
Physical Chemistry - Recent Methodologies in Biomolecular Spectroscopy
저자 및
공동저자
Jongcheol Seo
Department of Chemistry, Pohang University of Science and Technology, Korea
The protein topologies as well as structures, conformations are of great interest to the protein functions. Indeed, many different protein topologies are exist in nature, for example, a common linear string, a cyclic form, a threaded or extended lasso, a knotted or chained form and many more. Furthermore, an artificial proteins can be designed to have a specific topology, in order to engineer the protein functions. Thus, identifying and distinguishing such diverse topologies have a big significance for designing and characterizing such topologically-engineered proteins. In the present work, we implemented ion mobility-mass spectrometry (IM-MS) to investigate the topological as well as conformational transitions of specially-designed proteins (lasso-BXA) which can have a lasso topology. With IM-MS, we could distinguish different topologies and conformations of l-BXA, such as a threaded lasso and an extended tadpole, by measuring collision cross section values. Furthermore, transitions between threaded lasso and extended tadpole were observed upon collisional activation, which confirms the predicted topologies and conformations. Through this study, we have presented possibilities in examining the topological isomers of proteins with IM-MS. We expect this IM-MS approach may be established as a useful tool for studying protein topology.

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