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• W109084841 abstract "Different fluorescence spectroscopic approaches for the characterization of the peripheral membrane binding of proteins are summarized and compared for the blood coagulation protein prothrombin. Basically, the problem of membrane binding can be approached from both the protein side, using either intrinsic tryptophan fluorescence or dye-labeled protein, as typically employed in fluorescence recovery after photobleaching experiments, or from the membrane side, studying solvent relaxation, fluorescence anisotropy or excimer formation of suitable membrane probes. For the case of prothrombin and its fragment 1 the combined use of these fluorescence methods shows a slightly tighter binding of the fragment 1 portion in the case of the entire prothrombin molecule compared to the isolated fragment 1 while no evidence could be obtained for hydrophobic membrane binding sites in the “nonfragment 1” part of prothrombin. Tryptophan fluorescence of fragment 1 is able to detect differences in binding in response to the kind of procoagulant membrane lipid." @default.
• W109084841 created "2016-06-24" @default.
• W109084841 creator A5010915275 @default.
• W109084841 creator A5075121599 @default.
• W109084841 date "2002-01-01" @default.
• W109084841 modified "2023-09-27" @default.
• W109084841 title "Fluorescence Approaches for the Characterization of the Peripheral Membrane Binding of Proteins Applied for the Blood Coagulation Protein Prothrombin" @default.
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• W109084841 doi "https://doi.org/10.1007/978-3-642-56067-5_13" @default.
• W109084841 hasPublicationYear "2002" @default.
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