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  • 09월 10일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제124회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Probing Structural Change of Protein using Small-angle X-ray Scattering (SAXS) and Cross-linking Mass Spectrometry

2019년 8월 28일 14시 15분 00초
ANAL1.O-13 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
목 09시 : 36분
Analytical Chemistry - Oral Presentation of Young Analytical Chemists I
저자 및
Chae Eun Heo, Chae Ri Park, MyungKook Son, Sooyeon Chae, Min Ji Kim, Paul Valery Migisha Ntwali, Hugh I. Kim*
Department of Chemistry, Korea University, Korea
Probing the protein-protein interactions are crucial for the study of wide variety biological system. 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 influenced by PTM, metal ions, ion concentration has been reported that charged species abundant in our body (e.g. metal ion, DNA, nucleic acid, heparin, glycosaminoglycans etc.) influence to the mechanism of amyloid fibrillation by electrostatic interaction. Here, we have studied to understand the molecular mechanism of protein fibrillation under ATP, which is a small biological polyanion and is present in high levels in cell. Firstly, we have conducted the thioflavin T(ThT) assay which monitors the formation of amyloid fibril. To identify and characterize the protein complexes between protein and small molecules, we have utilized electrospray ionization mass spectrometry (ESI-MS) and ion mobility spectrometry (IMS), along with circular dichroism (CD) and solution small-angle x-ray scattering (SAXS). The experimental evidence obtained from these diverse analytical techniques, and subsequent studies about biological anion-mediated protein aggregation would be highly helpful in understanding the mechanistic details of amyloid fibrillation under the influence of external factors, which affect protein-protein interactions.