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Dataset showing the impact of the protonation states on molecular dynamics of HIV protease.

ABSTRACT: The data described here supports the research article "Unraveling HIV Protease Flaps Dynamics by Constant pH Molecular Dynamics Simulations" (Soares et al., 2016) [1]. The data involves both standard Molecular Dynamics (MD) and Constant pH Molecular Dynamics (CpHMD) to elucidate the effect of protonation states of catalytic dyad on the HIV-PR conformation. The data obtained from MD simulation demonstrate that the protonation state of the two aspartic acids (Asp25/Asp25') has a strong influence on the dynamics of the HIV-PR. Regarding the CpHMD simulation, we performed pka calculations for HIV-PR and the data indicate that only one catalytic aspartate should be protonated.

SUBMITTER: Soares RO

PROVIDER: S-EPMC4976645 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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Dataset showing the impact of the protonation states on molecular dynamics of HIV protease.

Soares Rosemberg O RO Torres Pedro H M PH da Silva Manuela L ML Pascutti Pedro G PG

Data in brief 20160725

The data described here supports the research article "Unraveling HIV Protease Flaps Dynamics by Constant pH Molecular Dynamics Simulations" (Soares et al., 2016) [1]. The data involves both standard Molecular Dynamics (MD) and Constant pH Molecular Dynamics (CpHMD) to elucidate the effect of protonation states of catalytic dyad on the HIV-PR conformation. The data obtained from MD simulation demonstrate that the protonation state of the two aspartic acids (Asp25/Asp25') has a strong influence o ...[more]

PMID: 27536715

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