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- W1969845747 abstract "We investigated the effects of four solutes on the protein rotational correlation time, the local dynamics of the protein backbone, and the mobility of labels covalently attached to multiple aqueous exposed sites in the HIV-1 protease (HIV-1 PR) using X-band continuous wave (CW) and pulsed electron paramagnetic resonance and fluorescence anisotropy. The HIV-1 PR contains two Beta-hairpin flaps that sit over the active site and are believed to undergo a large conformational change to allow the substrate access to the active site. The solutes used in this study were glycerol, sucrose, PEG3000 and Ficoll400 providing for a comparison between hydrophilic solutes (sucrose and Ficoll) and solutes that can interact with hydrophobic patches on the protein (glycerol and PEG3000) as well as a comparison between small viscogens and macromolecular crowders. The CW-EPR line shapes for four commonly used nitroxide spin labels attached to the Beta-hairpin flap region of HIV-1 protease were found to have to largest change in the presence of glycerol and PEG3000 whereas sucrose and glycerol have the larger affects on the steady-state fluorescence anisotropy. Comparison of the CW line shapes and distance distribution profiles from the pulsed EPR experiments for HIV-1 protease in the absence and presence of inhibitor reveals that the presence of solutes affects the line shape by perturbing the spin label mobility via preferential interactions between the solutes and the spin label." @default.
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- W1969845747 date "2009-02-01" @default.
- W1969845747 modified "2023-09-30" @default.
- W1969845747 title "Solute Effects on Spin Label Mobility for Aqueous Exposed Sites on HIV-1 Protease" @default.
- W1969845747 doi "https://doi.org/10.1016/j.bpj.2008.12.1547" @default.
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