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dc.contributor.authorPokhrel, Rudramani-
dc.contributor.authorPornthep Sompornpisut-
dc.contributor.authorChapagain, Prem-
dc.contributor.authorOlson, Brian-
dc.contributor.authorGerstman, Bernard-
dc.contributor.authorPandey, R. B.-
dc.contributor.otherChulalongkorn University. Faculty of Science-
dc.identifier.citationAIP Advances, Vol.8, No.12 (Dec., 2018) ; 8 pagesen_US
dc.description.abstractThe VP40 protein plays a critical role in coordinating the virion assembly, budding, and replication of the Ebola virus. Efforts have been made in recent years to understand various aspects of VP40 structure, dynamics, and function such as assembly of the protein and its roles in virus replication and penetration of the protein into the plasma membrane. A major conformational transformation is necessary for VP40 to form some of its oligomeric structures and to perform various functions. This conformational change from a compact structure with the N-terminal domain (NTD) and C-terminal domain (CTD) closely associated involves a dissociation or springing-out of the CTD from the NTD. We perform investigations using computational molecular dynamics simulations as well as knowledge-based Monte Carlo simulations. We find that a sharp springing of the CTD from the NTD in a free VP40 protein cannot occur solely by random thermal fluctuations without intermediate oligomerized segments, and therefore is likely triggered by additional molecular events.en_US
dc.publisherAmerican Institute of Physicsen_US
dc.rights© 2018 Author(s). All article content, except where otherwise noted, is licensed under a Creative Commons Attribution (CC BY) license (
dc.titleDomain rearrangement and denaturation in Ebola virus protein VP40en_US
dc.typeArticleen_US information provided- information provided- information provided- information provided- information provided-
Appears in Collections:Chula Scholars - 2018

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