Analysis of protein self-association at constant concentration by fluorescence-energy transfer
نویسندگان
چکیده
منابع مشابه
In vivo self-interaction of nodavirus RNA replicase protein a revealed by fluorescence resonance energy transfer.
Flock house virus (FHV) is the best-characterized member of the Nodaviridae, a family of small, positive-strand RNA viruses. Unlike most RNA viruses, FHV encodes only a single polypeptide, protein A, that is required for RNA replication. Protein A contains a C-proximal RNA-dependent RNA polymerase domain and localizes via an N-terminal transmembrane domain to the outer mitochondrial membrane, w...
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FRET microscopy enables the detection of different biochemical states of proteins in cells. The use of fluorescence in the detection of proteins, by chemical modification, by immunofluorescence, or by genetic encoding of a green fluorescent protein fusion protein, provides more information than just the location of the protein in the cell. The properties of the fluorophore can be exploited to e...
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In search of viable strategies to identify selective inhibitors of protein kinases, we have designed a binding assay to probe the interactions of human phosphoinositide-dependent protein kinase-1 (PDK1) with potential ligands. Our protocol is based on fluorescence resonance energy transfer (FRET) between semiconductor quantum dots (QDs) and organic dyes. Specifically, we have expressed and puri...
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متن کامل[13] Fluorescence Resonance Energy Transfer
of the extent of binding. This effect (known informally as "Chip dip") is illustrated in Figs. 6 and 7 which concern the ethidium bromide/tRNA system. 41 In this case the free ethidium bromide has a lifetime of 1.86 nsec and a rotational relaxation time of 0.54 nsec. On binding the PhetRNA Phe the lifetime increases to 26 nsec and the rotational relaxation increases to 136 nsec. A single rotati...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1998
ISSN: 0014-2956,1432-1033
DOI: 10.1046/j.1432-1327.1998.2550580.x