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

제116회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Expression, purification, and NMR Structural Studies of syndecan-4 as a transmembrane protein

2015년 8월 27일 16시 39분 56초
ANAL2.O-6 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
금 14시 : 57분
분석화학 - Oral Presentation of Young Analytical Chemists II
저자 및
김태형, 김지선*, 최성섭*, 김용애*
한국외국어대학교 화학과, Korea
Syndecans as cell surface receptors participate in biologically important cell-cell and cell-matrix interactions and interact with numerous potential ligands including growth factors and extracellular matrix molecules. The syndecan protein family has four members. One of them, Syndecan-4 is a protein that in humans is encoded by the syndecan-4 gene. They may affect tissue development and repair and growth-factors as well as the pathogenesis of numerous diseases, especially such as cancer. The transmembrane domain of syndecan-4 is consisted of 25 hydrophobic amino acids and involved in formation of dimer, which is crucial for transduction of signals. Thus, we demonstrated an optimized methods for recombinant expression and purification of syndecan-4(Syd4), mutant Syd4-TM(mSyd4) and Syd4-eTC. The mSyd4 has a partially modified sequence of wtSyd4 and Syd4-eTC has extracellular, transmembrane and cytoplasmic domain of syndecan-4. All peptides were purified by semi-preparative reversed-phase HPLC after cleaving the fusion partner with CNBr. Their biophysical properties of peptides were studied by circular dichroism (CD), mass spectrometry, and nuclear magnetic resonance (NMR) spectroscopy. CD spectra were presented that Syd4 analogues adopt a stable α-helical structure in micelle environments. Optimized structure of Syd4 analogues based on solution NMR spectroscopy and solid-state NMR spectroscopy based on 2D SAMPI4 were reinforced with Molecular Dynamics Simulation.