碩士 / 亞洲大學 / 生物資訊學系碩士班 / 97 / In this research is to study stability of Alzheimer’s disease-related amyloid protein, and to observe the difference of amyloid protein in different Oligomers.
This study used amyloid protein 2beg (17-24) structure, and the data resource came from RCSB protein data bank. CHARMM is the program that using in this study. For simulation and observation in 2beg(17-24) Monomer、Dimer and Pentamer in CHARMM, we need to setup simulation temperature in absolute temperature 300k for 2beg(17-24) Monomer、Dimer and Pentamer structure in water solution.
After simulation, we find out the total energy of monomer、Dimer and Pentamer are all stable. In analysis of Monomer、Dimer and Pentamer in RMSD and RMSF, Monomer has greatest displacement ,and Pentamer is most stable. In analysis of Monomer、Dimer and Pentamer in RGYR, all three structures have shrink phenomenon , and shrink phenomenon in monomer is most significance. Therefore, Monomer is the most unstable structure and also more easy to have polymerization.
| Identifer | oai:union.ndltd.org:TW/097THMU8112012 |
| Date | January 2009 |
| Creators | Chuen-Lin Hus, 許爵麟 |
| Contributors | Kuei-Jen Lee, 李桂仁 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 48 |
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