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FRET‐Capture: A Sensitive Method for the Detection of Dynamic Protein Interactions
Author(s) -
Socher Elke,
Imperiali Barbara
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200700
Subject(s) - förster resonance energy transfer , fluorophore , computer science , exploit , solvatochromism , chemistry , fluorescence , computational biology , biology , molecule , physics , computer security , organic chemistry , quantum mechanics
Caught in the act: The FRET‐Capture approach exploits a bound solvatochromic fluorophore, 4‐ N , N ‐dimethylamino‐1,8‐naphthalimide, as a FRET donor in both inter‐ and intramolecular energy transfer. A unique feature of this method is the additional level of signal selectivity as the FRET signal is only turned on when the donor is specifically bound to the protein of interest, eliminating high background and false positive signals.

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