https://scholars.lib.ntu.edu.tw/handle/123456789/598257
標題: | Insights to Human γD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations | 作者: | Hsueh S.-S Wang S.S.-S Chen S.-H Wang C.-L Wu J.W Lin T.-H. STEVEN SHENG-SHIH WANG |
關鍵字: | Aggregation;Cataract;Human γD-crystallin;Molecular dynamics simulations;NMR spectroscopy;Stability;Unfolding | 公開日期: | 2022 | 卷: | 23 | 期: | 3 | 來源出版物: | International Journal of Molecular Sciences | 摘要: | Human γD-crystallin (HGDC) is an abundant lens protein residing in the nucleus of the human lens. Aggregation of this and other structural proteins within the lens leads to the development of cataract. Much has been explored on the stability and aggregation of HGDC and where detailed investigation at the atomic resolution was needed, the X-ray structure was used as an initial starting conformer for molecular modeling. In this study, we implemented NMR-solution HGDC structures as starting conformers for molecular dynamics simulations to provide the missing pieces of the puzzle on the very early stages of HGDC unfolding leading up to the domain swap theories proposed by past studies. The high-resolution details of the conformational dynamics also revealed additional insights to possible early intervention for cataractogenesis. ? 2022 by the authors. Licensee MDPI, Basel, Switzerland. |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85123537843&doi=10.3390%2fijms23031591&partnerID=40&md5=ae7e050c8cfbf0cf2f97d5c0436b99d7 https://scholars.lib.ntu.edu.tw/handle/123456789/598257 |
ISSN: | 16616596 | DOI: | 10.3390/ijms23031591 |
顯示於: | 化學工程學系 |
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