Physical properties of the HIV-1 capsid from all-atom molecular dynamics simulations [electronic resource].
- Published
- Oakland, Calif. : United States. Dept. of Energy. Oakland Operations Office, 2017.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy - Physical Description
- Article numbers 15,959 : digital, PDF file
- Additional Creators
- Battelle Memorial Institute, United States. Department of Energy. Oakland Operations Office, Oak Ridge National Laboratory, United States. Department of Energy. Office of Science, National Institutes of Health (U.S.), and United States. Department of Energy. Office of Scientific and Technical Information
Access Online
- Restrictions on Access
- Free-to-read Unrestricted online access
- Summary
- Human immunodeficiency virus type 1 (HIV-1) infection is highly dependent on its capsid. The capsid is a large container, made of B 1,300 proteins with altogether 4 million atoms. Though the capsid proteins are all identical, they nevertheless arrange themselves into a largely asymmetric structure made of hexamers and pentamers. The large number of degrees of freedom and lack of symmetry pose a challenge to studying the chemical details of the HIV capsid. Simulations of over 64 million atoms for over 1 μs allow us to conduct a comprehensive study of the chemical–physical properties of an empty HIV-1 capsid, including its electrostatics, vibrational and acoustic properties, and the effects of solvent (ions and water) on the capsid. Furthermore, the simulations reveal critical details about the capsid with implications to biological function.
- Report Numbers
- E 1.99:1393179
- Subject(s)
- Note
- Published through SciTech Connect.
07/19/2017.
"ncomms15959"
Nature Communications 8 ISSN 2041-1723 AM
Juan R. Perilla; Klaus Schulten. - Funding Information
- AC05-00OR22725
9P41GM104601
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