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• W1978466327 abstract "Chemical proteomics aims to characterize all of the proteins in the proteome with respect to their function, which is associated with their interaction with other molecules. We propose the identification of a subproteomic library of expressed proteins whose native structures are typified by the presence of hydrophobic surface sites, which are often involved in interactions with small molecules, membrane lipids, and other proteins, pertaining to their functions. We demonstrate that soluble globular proteins with hydrophobic surface sites can be detected selectively by staining on an electrophoretic gel run under nondenaturing conditions. The application of these staining techniques may help elucidate new catalytic, transport, and regulatory functionalities in complex proteomic screenings." @default.
• W1978466327 created "2016-06-24" @default.
• W1978466327 creator A5018709673 @default.
• W1978466327 creator A5042062773 @default.
• W1978466327 date "2003-08-16" @default.
• W1978466327 modified "2023-10-17" @default.
• W1978466327 title "Selective Staining of Proteins with Hydrophobic Surface Sites on a Native Electrophoretic Gel" @default.
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• W1978466327 doi "https://doi.org/10.1021/pr025579+" @default.
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