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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lee, Myeongsang Chang, Hyun Joon Park, Jung Yeon Shin, Joonha Park, Jong Woo Choi, Jee Woo Kim, Jae In Na, Sungsoo |
| Description | Author Affiliation: Lee M ( Department of Mechanical Engineering, Korea University, Seoul 02481, Republic of Korea.); Chang HJ ( Department of Mechanical Engineering, Korea University, Seoul 02481, Republic of Korea.); Park JY ( Seoul Science High School, Seoul 03066, Republic of Korea.); Shin J ( Seoul Science High School, Seoul 03066, Republic of Korea.); Park JW ( Seoul Science High School, Seoul 03066, Republic of Korea.); Choi JW ( Seoul Science High School, Seoul 03066, Republic of Korea.); Kim JI ( Department of Mechanical Engineering, Korea University, Seoul 02481, Republic of Korea. Electronic address: jay414@korea.ac.kr.); Na S ( Department of Mechanical Engineering, Korea University, Seoul 02481, Republic of Korea. Electronic address: nass@korea.ac.kr.) |
| Abstract | Amyloid proteins are known to be the main cause of numerous degenerative and neurodegenerative diseases. In general, amyloids are misfolded from monomers and they tend to have ß-strand formations. These misfolded monomers are then transformed into oligomers, fibrils, and plaques. It is important to understand the forming mechanism of amyloids in order to prevent degenerative diseases to occur. Aß protein is a highly noticeable protein which causes Alzheimer's disease. It is reported that solvents affect the forming mechanism of Aß amyloids. In this research, Aß1-42 was analyzed using an all-atom MD simulation with the consideration of effects induced by two disparate solvents: water and DMSO. As a result, two different conformation changes of Aß1-42 were exhibited in each solvent. It was found that salt-bridge of Asp23 and Lys28 in Aß1-42 was the key for amyloid folding based on the various analysis including hydrogen bond, electrostatic interaction energy and salt-bridge distance. Since this salt-bridge region plays a crucial role in initiating the misfolding of Aß1-42, this research may shed a light for studies related in amyloid folding and misfolding. |
| File Format | HTM / HTML |
| ISSN | 10933263 |
| Journal | Journal of Molecular Graphics and Modelling |
| Volume Number | 65 |
| e-ISSN | 18734243 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-04-01 |
| Publisher Place | United States |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Computer Graphics and Computer-Aided Design Spectroscopy Materials Chemistry Physical and Theoretical Chemistry |
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