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- W4240051585 abstract "'The overall goal of the research is to apply the methods of structural biology, which have been previously used primarily in biomedical applications, to bioremediation. The authors are doing this by using NMR spectroscopy to determine the structures of proteins involved in the bacterial mercury detoxification system. The research is based on the premise that the proteins encoded in the genes of the bacterial detoxification system are an untapped source of reagents and, more fundamentally, chemical strategies that can be used to remove heavy metal toxins from the environment. The initial goals are to determine the structures of the proteins of the bacterial mercury detoxification systems responsible for the sequestration and transport of the Hg(II) ions in to the cell where reduction to Hg(O) occurs. These proteins are meP, which is water soluble and can be investigated with multidimensional solution NMR methods, and merT, the transport protein in the membrane that requires solid-state NMR methods. As of June 1998, this report summarizes work after about one and half years of the three-year award. The authors have made significant accomplishments in three aspects of the NMR studies of the proteins of the bacterial mercury detoxification system.'" @default.
- W4240051585 created "2022-05-12" @default.
- W4240051585 creator A5091221111 @default.
- W4240051585 date "1998-06-01" @default.
- W4240051585 modified "2023-09-27" @default.
- W4240051585 title "Structural biology of the sequestration and transport of heavy metal toxins: NMR structure determination of roteins containing the -Cys-X-Y-Cys-metal binding motifs. 1998 annual progress report" @default.
- W4240051585 doi "https://doi.org/10.2172/13584" @default.
- W4240051585 hasPublicationYear "1998" @default.
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