| 학회 | 한국고분자학회 |
| 학술대회 | 2005년 봄 (04/14 ~ 04/15, 전경련회관) |
| 권호 | 30권 1호, p.15 |
| 발표분야 | 나노구조형 고분자 분광분석 |
| 제목 | Solid-state NMR Studies of Membrane Proteins |
| 초록 | Approximately 30% of all expressed polypeptides are membrane-associated but neither X-ray crystallography nor solution NMR spectroscopy is very effective for these proteins. The lipids required for the structural integrity and functionality of membrane proteins impede crystallization as well as the rate of overall reorientation in solution. Solid-state NMR experiments on lipid bilayer samples are especially valuable for membrane proteins with predominantly helical secondary structure. High resolution solid-state NMR spectroscopy is capable of determining the backbone and side chain structures of membrane proteins. The nicotinic acetylcholine receptor (nAChR) from Torpedo is an abundant neurotransmitter-gated ion channel that is used extensively as a structural model for homologous ligand-gated channels located throughout the central and peripheral nervous systems. The nAChR is composed of four subunits organized pseudo-symmetrically as a pentamer around a central ion channel pore. The four transmembrane segments (M1, M2, M3, and M4) form the ion channel pore, with M2 from each subunit directly lining the ion channel. To get a better understanding of the structure of M2, we cloned, expressed, purified, and isolated M2 peptide. Mutant E.coli strain of C41(DE3) was used and the yield is 250mg/1L growth with a fusion partner KSI. Membrane bound structure of M2 in micelle was studied by solution NMR spectroscopy (600MHz) using HSQC, HSQC-NOSEY, and IPAP-HSQC in a compressed gel and a stretched gel. Membrane bound structure of M2 was studied by solid-state NMR spectroscopy (700MHz) in an oriented bicelles samples using 2D PISEMA, PISA Wheel, and Structural fittings. |
| 저자 | YONGAE KIM |
| 소속 | Dept. of Chemistry |
| 키워드 | Solid-state NMR; Membrane Proteins; Solution NMR; 2D PISEMA; PISA Wheel |
