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• W2738606079 abstract "Human immunodeficiency virus type 1 (HIV-1) infection is highly dependent on its capsid. The capsid is a large container, made of ∼1,300 proteins with altogether 4 million atoms. Although 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. The simulations reveal critical details about the capsid with implications to biological function." @default.
• W2738606079 created "2017-07-31" @default.
• W2738606079 creator A5029996336 @default.
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• W2738606079 date "2017-07-19" @default.
• W2738606079 modified "2023-10-14" @default.
• W2738606079 title "Physical properties of the HIV-1 capsid from all-atom molecular dynamics simulations" @default.
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• W2738606079 doi "https://doi.org/10.1038/ncomms15959" @default.
• W2738606079 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5524983" @default.
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• W2738606079 hasPublicationYear "2017" @default.
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